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Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase
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EC Tree
2.7.8.7 holo-[acyl-carrier-protein] synthaseIUBMB Comments
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain . The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty-acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes . Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
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Word Map
- 2.7.8.7
-
phosphopantetheinylation
- polyketide
-
4\'-phosphopantetheinyl
-
nonribosomal
- synthetases
-
peptidyl
-
siderophore
-
lipopeptide
-
nrpss
- apo-acp
- enterobactin
-
holo-forms
-
biosurfactant
-
fengycin
-
indigoidine
- biotechnology
- alpha-aminoadipate
- analysis
- drug development
- molecular biology
- medicine
- synthesis
-
iturins
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
+
an apo-[acyl-carrier protein]
=
+
Synonyms
pptase, phosphopantetheinyl transferase, surfactin synthetase, 4'-phosphopantetheinyl transferase, mtppt, type ii fatty acid synthase system, sfp-type pptase, schppt, holo-acyl carrier protein synthase, mtacps, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(FAS)ACP
4'-phosphopantetheinyl transferase
4-phosphopantetheinyl transferase
AcpS
acyl carrier protein holoprotein (holo-ACP) synthetase
-
-
-
-
acyl carrier protein synthase
acyl carrier protein synthetase
-
-
-
-
BcPPT
BPSS2266
coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase
-
-
-
-
EntD
FKACPS
FKPPT1
FKPPT2
FKPPT3
FKPPT4
holo ACP synthase
holo-ACP synthase
holo-ACP synthetase
-
-
-
-
holo-acyl carrier protein synthase
holosynthase
-
-
-
-
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
UniProt
NpgA
P-pant transferase
PcpS
phosphopantetheinyl transferase
PP1183
PPT
PPT1
PPTase
PptB
PptT
PswP
PTase
Rv2794c
SchPPT
Sfp
sfp lpa-8
Sfp-type PPTase
surfactin phosphopantetheinyl transferase
type-II PPTase PptT
VabD
XabA
AcpS
-
acyl carrier protein synthases that recognize carrier protein from primary metabolism
holo-ACP synthase
-
-
-
-
phosphopantetheinyl transferase
close to the class two phosphopantetheinyl transferase Sfp from Bacillus subtilis
phosphopantetheinyl transferase
-
phosphopantetheinyl transferase
-
phosphopantetheinyl transferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CoA-[4'-phosphopantetheine] + an apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier protein]
CoA-[4'-phosphopantetheine] + an apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier protein]
-
-
-
-
CoA-[4'-phosphopantetheine] + an apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier protein]
sequential binding mechanism: initial CoA- and Mg2+-binding followed by binding of acyl-carrier protein (ACP), nucleophilic attack of ACP-serine-hydroxylate on beta-phosphate of CoA followed by charge migration, Lys185-protonation, diphosphate-cleavage, and product dissociation, rate limiting step: release of 3',5'-ADP, key acid/base catalysts: residues E181 (CoA-binding) and K185 (Mg2+-binding)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
CoA-[4'-phosphopantetheine]:apo-[acyl-carrier protein] 4'-pantetheinephosphotransferase
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty-acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
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CAS REGISTRY NUMBER
COMMENTARY
37278-30-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxybutanoyl-CoA + apo-[acyl-carrier protein]
CoA + 3-hydroxybutanoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
7-nitrobenz-2-oxa-1,3-diazol-4-yl-CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + 7-nitrobenz-2-oxa-1,3-diazol-4-yl-holo-[acyl-carrier protein]
acetoacetyl-CoA + apo-[acyl-carrier protein]
CoA + acetoacetyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
apo-[acyl-carrier protein] + acetyl-CoA
CoA + acetyl-[acyl-carrier protein]
pH 7, 37°C
reaction stop by 10% trichloroacetic acid, limited release of 3,5-ADP by interactions with guanidinium moieties of R74 and R86
-
?
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
-
-
-
-
r
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
butanoyl-CoA + apo-[acyl-carrier protein]
CoA + butanoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
-
-
-
-
r
CoA + apo-[fredericamycin H acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[fredericamycin acyl-carrier protein]
-
-
-
?
CoA + apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
? + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
CoA + apo-[peptidyl-carrier protein 1]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
?
CoA + apo-[peptidyl-carrier protein 2]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
?
CoA + apo-[peptidyl-carrier protein 3]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
?
CoA + apo-[peptidyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
?
CoA + apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. granaticin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
-
-
-
r
CoA + apo-[tetracenomycin M acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[tetracenomycin M acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
CoA-[4'-phosphopantetheine] + apo-[EntB-ArCP-H6 Escherichia coli]
?
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[FDH protein]
adenosine 3',5'-bisphosphate + holo-[FDH protein]
-
the enzyme modifies the apo-FDH protein at serine 354 and activates its catalysis
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
CoA + crotonyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
desulfoCoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
? + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
-
-
-
r
dodecanoyl-CoA + apo-[acyl-carrier protein]
CoA + dodecanoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
lauroyl-CoA + apo-[acyl-carrier protein]
CoA + lauroyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
myristoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
myristoyl-CoA + apo-[acyl-carrier protein]
CoA + myristoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
palmitoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoyl-CoA + apo-[acyl-carrier protein]
CoA + palmitoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
phenylacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
7-nitrobenz-2-oxa-1,3-diazol-4-yl-CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + 7-nitrobenz-2-oxa-1,3-diazol-4-yl-holo-[acyl-carrier protein]
-
-
-
?
7-nitrobenz-2-oxa-1,3-diazol-4-yl-CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + 7-nitrobenz-2-oxa-1,3-diazol-4-yl-holo-[acyl-carrier protein]
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
substrate for isoform AcpS
-
-
?
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
substrate for isoform AcpS
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
r
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
recombinant enzyme
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
substrate for isoform Sfp
-
-
?
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
-
-
-
-
?
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
-
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
-
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
-
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
recombinant enzyme
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
transfers 4'-phosphopantetheine from reduced coenzyme A to acyl carrier proteon apoprotein
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Dcp from Lactobacillus casei, NodF from Rhizobium leguminosarum and several polyketide synthase ACPs from Streptomyces sp. also serves as substrates
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Streptomycess sp. acyl carrier proteins and coenzyme A analogs also serves as substrates for holo-ACP synthase in vitro
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
transfers 4'-phosphopantetheine from reduced coenzyme A to acyl carrier proteon apoprotein
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme in volved in lysine catabolism
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme involved in lysine catabolism
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
assay with wild-type and mutant ACP substrates from Leishmania major (LmACP), mutants N35D, F44M, and F44A, the double mutants N35D/F44M and N35D/Q48E, triple mutant N35D/F44M/Q48E of LmACP, and with Escherichia coli ACP, the M44F mutant of Escherichia coli ACP, Plasmmodium falciparum ACP, and Mycobacterium tuberculosis ACP. No activity with LmACP F44A mutant
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
assay with wild-type and mutant ACP substrates from Leishmania major (LmACP), mutants N35D, F44M, and F44A, the double mutants N35D/F44M and N35D/Q48E, triple mutant N35D/F44M/Q48E of LmACP, and with Escherichia coli ACP, the M44F mutant of Escherichia coli ACP, Plasmmodium falciparum ACP, and Mycobacterium tuberculosis ACP. No activity with LmACP F44A mutant
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS)
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
PPTase cleaves coenzyme A, transfers the P-pant moiety to a conserved residue of inactive substrates, and produces 3'5'-ADP
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
PPTase cleaves coenzyme A, transfers the P-pant moiety to a conserved residue of inactive substrates, and produces 3'5'-ADP
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme activates the siderophore petrobactin. The synthase-encoding cluster contains a stand-alone PCP domain, AsbD, which is phosphopantetheinylated by a PPTase. There is no PPTase present in the gene cluster itself and it is suggested that BA2375, an EntD homologue present in the enterobactin gene cluster, serves as the PPTase that installs the 4'-phosphopantetheinyl arm on AsbD. Holo-AsbD is loaded with 3,4-dihydroxybenzoic acid by AsbC and this AsbD conjugate functions as the substrate for AsbE. AsbE, together with the stand-alone synthases AsbA and AsbB, catalyze the formation of petrobactin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme activates bacitracin and in vitro also tyrocidin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme Sfp is active with surfactin synthase peptidyl carrier protein
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme Sfp is active with surfactin synthase peptidyl carrier protein
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
catalytic activity of Ppt2 as a phosphopantetheinyl transferase and the acyl carrier protein Acp1 as a substrate, Acp12 is no substrate. The terminal thiol group of the 4'PPT is the site at which elongation occurs via thioester linkages and attachments are covalently linked
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme recognizes the apo-[acyl-carrier protein] from Clamydomonas reinhardtii and weakly that of Escherichia coli
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme recognizes the apo-[acyl-carrier protein] from Clamydomonas reinhardtii, Escherichia coli and actinorhodin ACP
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the carrier protein of Colibactin is phosphopantetheinylated by the family II PPTase ClbA
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the carrier protein of the enterobactin synthase complex, EntF, is phosphopantetheinylated by the family II PPTase EntD. In vitro EntD seems to modify apo-AcpP from Escherichia coli, albeit at a very slow rate
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme AcpS is active with type II FAS ACP, AcpP, but the enzyme accepts not only bacterial AcpP but a variety of CPs from type II elongating systems including Lactobacillus casei D-alanyl carrier protein, Rhizobia protein NodF and Streptomyces ACPs involved in frenolicin, granaticin, oxytetracycline and tetracenomycin polyketide biosynthesis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme Sfp is active with surfactin synthase peptidyl carrier protein. Sfp shows highly permissive catalytic activity towards CPs using not only CoA but CoA-like substrates
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
assay with ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens. The structure of the holo-acyl carrier protein of Leishmania major is similar to other type II ACPs, comprising a four-helix bundle, enclosing a hydrophobic core, but it displays a remarkably different phosphopantetheinyl transferase binding interface. Two- and three-dimensional NMR structure analysis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
with the most soluble and compact ACP fragment (2042-2188) of ACP substrate from the type I polyketide synthase PpsC from Mycobacterium tuberculosis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
with the most soluble and compact ACP fragment (2042-2188) of ACP substrate from the type I polyketide synthase PpsC from Mycobacterium tuberculosis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
broad specificity of the single PPTase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
broad specificity of the single PPTase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Serratia marcescens Db11
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
usage of ACP substrate kbB-ACP4, an ACP in FK506 biosynthetic PKS/NRPS hybrid from Streptomyces tsukubaensis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
usage of ACP substrate kbB-ACP4, an ACP in FK506 biosynthetic PKS/NRPS hybrid from Streptomyces tsukubaensis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The carrier protein tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
both VibB and VibF are phosphopantetheinylated by the PPTase VibD
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q74V64
the enzyme activates yersiniabactin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
additional information
?
-
analysis of enzyme activities with three recombinant apo-mtACP isoforms, i.e. mtACP1 (AT2G44620), mtACP2 (AT1G65290) and mtACP3 (AT5G47630), overview
-
-
?
additional information
?
-
analysis of enzyme activities with three recombinant apo-mtACP isoforms, i.e. mtACP1 (AT2G44620), mtACP2 (AT1G65290) and mtACP3 (AT5G47630), overview
-
-
?
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
?
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
?
additional information
?
-
-
Sfp type exhibits an extraordinarily broad substrate specificity
-
-
?
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
?
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
?
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
?
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
?
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
?
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
?
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
?
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
?
additional information
?
-
-
mutant ACP in which the target serine 36 has been mutated to a threonine residue is an inactive substrate for phosphopantetheinylation
-
-
?
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
?
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
?
additional information
?
-
-
isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
-
-
?
additional information
?
-
besides enterobactin and colibactin, some Escherichia coli strains also produce yersiniabactin. Yersiniabactin is encoded by the high-pathogenicity island and in contrast to Yersinia pestis (in Yersinia pestis YbtD is the dedicated PPTase) no PPTase is found in the Escherichia coli genome that seems to activate this synthase
-
-
?
additional information
?
-
besides enterobactin and colibactin, some Escherichia coli strains also produce yersiniabactin. Yersiniabactin is encoded by the high-pathogenicity island and in contrast to Yersinia pestis (in Yersinia pestis YbtD is the dedicated PPTase) no PPTase is found in the Escherichia coli genome that seems to activate this synthase
-
-
?
additional information
?
-
besides enterobactin and colibactin, some Escherichia coli strains also produce yersiniabactin. Yersiniabactin is encoded by the high-pathogenicity island and in contrast to Yersinia pestis (in Yersinia pestis YbtD is the dedicated PPTase) no PPTase is found in the Escherichia coli genome that seems to activate this synthase
-
-
?
additional information
?
-
besides enterobactin and colibactin, some Escherichia coli strains also produce yersiniabactin. Yersiniabactin is encoded by the high-pathogenicity island and in contrast to Yersinia pestis (in Yersinia pestis YbtD is the dedicated PPTase) no PPTase is found in the Escherichia coli genome that seems to activate this synthase
-
-
?
additional information
?
-
carrier proteins from type I elongating systems are not substrates for AcpS. Inability of Escherichia coli AcpS to install a PPant arm on apo-EntF, the bacterial enterobactin synthase, or apo-TycA, the Bacillus brevis tyrocidine synthase
-
-
?
additional information
?
-
carrier proteins from type I elongating systems are not substrates for AcpS. Inability of Escherichia coli AcpS to install a PPant arm on apo-EntF, the bacterial enterobactin synthase, or apo-TycA, the Bacillus brevis tyrocidine synthase
-
-
?
additional information
?
-
carrier proteins from type I elongating systems are not substrates for AcpS. Inability of Escherichia coli AcpS to install a PPant arm on apo-EntF, the bacterial enterobactin synthase, or apo-TycA, the Bacillus brevis tyrocidine synthase
-
-
?
additional information
?
-
carrier proteins from type I elongating systems are not substrates for AcpS. Inability of Escherichia coli AcpS to install a PPant arm on apo-EntF, the bacterial enterobactin synthase, or apo-TycA, the Bacillus brevis tyrocidine synthase
-
-
?
additional information
?
-
ACPS accepts very efficiently acyl-CoAs with chain lengths up to C16, and with decreasing activity also longer chains (C18 to C20)
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
?
additional information
?
-
-
single broad specificity enzyme for all posttranslational 4'-phosphopantetheinylation reactions, also capable of phosphopantetheinylation of peptidyl carrier and acyl carrier proteins from prokaryotes
-
-
?
additional information
?
-
development of a direct and continuous assay for this enzyme class based upon monitoring polarization of a fluorescent phosphopantetheine analogue as it is transferred from a low molecular weight coenzyme A substrate to higher molecular weight protein acceptor, utility of the method for the biochemical characterization of phosphopantetheinyl transferase Sfp, a canonical enzyme, recombinant enzyme with substrates VibB and 90 amino acid ACP (hACP) from human fatty acid synthase, overview
-
-
?
additional information
?
-
-
development of a direct and continuous assay for this enzyme class based upon monitoring polarization of a fluorescent phosphopantetheine analogue as it is transferred from a low molecular weight coenzyme A substrate to higher molecular weight protein acceptor, utility of the method for the biochemical characterization of phosphopantetheinyl transferase Sfp, a canonical enzyme, recombinant enzyme with substrates VibB and 90 amino acid ACP (hACP) from human fatty acid synthase, overview
-
-
?
additional information
?
-
recombinant expression of ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens in Escherichia coli and purification by ion exchange chromatography. LmACP does not interact with the bacterial group I, 4'-phosphopantetheinyl transferase. Residues Asn 35 and Phe 44, present in LmACP modulate its interaction with AcpS
-
-
?
additional information
?
-
-
recombinant expression of ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens in Escherichia coli and purification by ion exchange chromatography. LmACP does not interact with the bacterial group I, 4'-phosphopantetheinyl transferase. Residues Asn 35 and Phe 44, present in LmACP modulate its interaction with AcpS
-
-
?
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
?
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
?
additional information
?
-
-
SePptII is active in phosphopantetheinyl transfer with an acyl carrier protein-thioesterase didomain from the erythromycin polyketide synthase as substrate. SePptII provides complete modification of acyl-carrier protein-thioesterase and of an entire multienzymne subunit from the erythromycin polyketide synthase
-
-
?
additional information
?
-
phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP
-
-
?
additional information
?
-
-
phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP
-
-
?
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
?
additional information
?
-
activates polyketide synthases and polypetide synthases, processes an aryl carrier protein domain ArCP, derived from the enterobactin synthetase of Escherichia coli, as well as a peptidyl carrier protein domain from a polypeptide synthase of yet unknown function from Sorangium cellulosum
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
substrate promiscuity of the phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins, SchPPT has a broad substrate specificity for ACPs
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
?
additional information
?
-
substrate promiscuity of the phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins, SchPPT has a broad substrate specificity for ACPs
-
-
?
additional information
?
-
-
substrate promiscuity of the phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins, SchPPT has a broad substrate specificity for ACPs
-
-
?
additional information
?
-
enzyme is involved in fredericamycin biosynthesis
-
-
?
additional information
?
-
-
enzyme is involved in fredericamycin biosynthesis
-
-
?
additional information
?
-
Streptomyces pneumoniae
dephospho-CoA is no substrate
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
?
additional information
?
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
?
additional information
?
-
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
?
additional information
?
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
?
additional information
?
-
Escherichia coli ACP and mutant ACP proteins rACP, V12G, F50A, I54L, I154V, A59G and Y71A are substrates, mutant I54A is no substrate
-
-
?
additional information
?
-
-
D35 in site A of acyl carrier protein is critical for enzyme activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme involved in lysine catabolism
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
-
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS)
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme activates the siderophore petrobactin. The synthase-encoding cluster contains a stand-alone PCP domain, AsbD, which is phosphopantetheinylated by a PPTase. There is no PPTase present in the gene cluster itself and it is suggested that BA2375, an EntD homologue present in the enterobactin gene cluster, serves as the PPTase that installs the 4'-phosphopantetheinyl arm on AsbD. Holo-AsbD is loaded with 3,4-dihydroxybenzoic acid by AsbC and this AsbD conjugate functions as the substrate for AsbE. AsbE, together with the stand-alone synthases AsbA and AsbB, catalyze the formation of petrobactin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Serratia marcescens Db11
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The carrier protein tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
both VibB and VibF are phosphopantetheinylated by the PPTase VibD
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q74V64
the enzyme activates yersiniabactin
-
-
?
additional information
?
-
-
isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
-
-
?
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
?
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
?
additional information
?
-
phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP
-
-
?
additional information
?
-
-
phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP
-
-
?
additional information
?
-
enzyme is involved in fredericamycin biosynthesis
-
-
?
additional information
?
-
-
enzyme is involved in fredericamycin biosynthesis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
dependent on, binding structure, overview. The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
additional information
-
Ca2+, Fe2+, Co2+ and Zn2+ are ineffective, inhibitory or both, at intermediate and high concentrations
additional information
-
CuSO4, CdCl2 and CrCl2 does not stimulate the reaction at any ceoncentration, trivalent metal cations such as FeCl3 or AlCl3 are ineffective
additional information
Mg2+ results in the highest activity among the divalent ions tested followed by Mn2+, while Ca2+ has no effect on the activity of the enzyme
additional information
-
Mg2+ results in the highest activity among the divalent ions tested followed by Mn2+, while Ca2+ has no effect on the activity of the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
-
IC50: 0.0021 mM
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.015 mM
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0015 mM
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0034 mM
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.002 mM
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00013 mM
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0011 mM
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0019 mM
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0013 mM
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00027 mM
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0044 mM
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00083 mM
apo-acyl-carrier protein
-
mutant ACP in which the target serine 36 has been mutated to a threonine residue is an inhibitor as well as an inactive substrate
additional information
-
no substantial inhibition of Sfp by apo-[PCPH6SrfB1.18]
-
additional information
no or poor inhibition by Bay 11-7085, benserazide, (-)-ephedrine hemisulfate, and mitoxantrone
-
additional information
-
no or poor inhibition by Bay 11-7085, benserazide, (-)-ephedrine hemisulfate, and mitoxantrone
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
apo-acyl-carrier protein
Streptomyces pneumoniae
significantly stimulating above 0.01 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Microcephaly
Mitochondrial uptake of thiamin pyrophosphate: physiological and cell biological aspects.
Tuberculosis
4'-Phosphopantetheinyl transferase PptT, a new drug target required for Mycobacterium tuberculosis growth and persistence in vivo.
Tuberculosis
AcpM, the meromycolate extension acyl carrier protein of Mycobacterium tuberculosis, is activated by the 4'-phosphopantetheinyl transferase PptT, a potential target of the multistep mycolic acid biosynthesis.
Tuberculosis
Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.
Tuberculosis
Detection of soluble co-factor dependent protein expression in vivo: Application to the 4'-phosphopantetheinyl transferase PptT from Mycobacterium tuberculosis.
Tuberculosis
Inhibition of Indigoidine Synthesis as a High-Throughput Colourimetric Screen for Antibiotics Targeting the Essential Mycobacterium tuberculosis Phosphopantetheinyl Transferase PptT.
Tuberculosis
Insights from the docking and molecular dynamics simulation of the Phosphopantetheinyl transferase (PptT) structural model from Mycobacterium tuberculosis.
Tuberculosis
Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis.
Tuberculosis
Mass spectral determination of phosphopantetheinylation specificity for carrier proteins in Mycobacterium tuberculosis.
Tuberculosis
Negative regulation by Ser/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system.
Tuberculosis
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
Tuberculosis
Structural insights into phosphopantetheinyl hydrolase PptH from Mycobacterium tuberculosis.
Tuberculosis
Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of mycobacteria.
Tuberculosis
The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37°C, Escherichia coli acyl carrier protein
0.005
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37°C, Escherichia coli acyl carrier protein
0.039
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
pH 7.0, 37°C, Escherichia coli acyl carrier protein
0.022
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
pH 7.0, 37°C, Escherichia coli acyl carrier protein
0.021
apo-ACP
-
pH 7.0, 37°C, Bacillus subtilis acyl carrier protein-A as substrate
0.0002
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme AcpS, 0.002-0.008 mM substrate
0.0013
apo-acyl-carrier protein
Streptomyces pneumoniae
pH 7.0, 37°C, trichloroacetic acid precipitation method
0.0014
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme Sfp, 0.002-0.008 mM substrate
0.002
apo-acyl-carrier protein
-
pH 7.0, 37°C, Escherichia coli acyl carrier protein
0.003
apo-acyl-carrier protein
pH 7.8, 37°C, mutant acyl carrier protein Y71A
0.0031
apo-acyl-carrier protein
-
pH 7.0, 37°C, human acyl carrier protein f as as substrate
0.0073
apo-acyl-carrier protein
pH 7.8, 37°C, mutant acyl carrier protein V12G
0.0075
apo-acyl-carrier protein
-
pH 7.0, 37°C, human acyl carrier protein mit as substrate
0.0094
apo-acyl-carrier protein
pH 7.8, 37°C, Escherichia coli acyl carrier protein
0.013
apo-acyl-carrier protein
pH 7.8, 37°C, mutant acyl carrier protein A59G
0.029
apo-acyl-carrier protein
pH 7.8, 37°C, mutant acyl carrier protein I54L
0.0216
apo-peptidyl carrier protein
-
pH 8.8, 37°C, isoenzyme AcpS, apo-hPCP
0.0038
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant F44M ACP substrate from Leishmania major
0.0048
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/Q48E ACP substrate from Leishmania major
0.00524
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M ACP substrate from Leishmania major
0.0055
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M/Q48E ACP substrate from Leishmania major
0.0063
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, wild-type ACP substrate from Leishmania major
0.0269
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D ACP substrate from Leishmania major
0.101
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Mycobacterium tuberculosis
0.12
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli ACP substrate
0.13
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli mutant M44F ACP substrate
0.215
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Plasmodium falciparum
0.0071
CoA
Streptomyces pneumoniae
pH 7.0, 37°C, trichloroacetic acid precipitation method
0.0038
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
additional information
acetyl-CoA
double mutant Q112E, E181Q, Kcat/KM: 0.2 1/min/mM
additional information
acetyl-CoA
-
double mutant Q112E, E181Q, Kcat/KM: 0.2 1/min/mM
additional information
Mg2+
mutant Q112E, E181Q, Kcat/KM: 0.0002 1/min/mM
additional information
additional information
-
KM-values numbers with mutants of peptidyl-carrier protein as substrate
-
additional information
additional information
quantitative kinetic measurements, steady-state kinetics
-
additional information
additional information
holo-ACPP binds the enzyme with greater affinity than the substrate, apo-ACPP, and with negative cooperativity. Cooperativity is not observed for apo-ACPP
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.317
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37°C, E. coli ACP
0.5
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37°C, E. coli ACP
0.167
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
pH 7.0, 37°C, E. coli ACP
0.09
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
pH 7.0, 37°C, E. coli ACP
0.0283
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme Sfp, 0.002-0.008 mM substrate
0.208
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme Sfp, 0.02-0.2 mM substrate
0.367
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme AcpS, 0.002-0.008 mM substrate
2.08
apo-acyl-carrier protein
-
pH 8.8, 37°C, isoenzyme AcpS, 0.02-0.2 mM substrate
0.239
apo-peptidyl carrier protein
-
pH 8.8, 37°C, isoenzyme AcpS, apo-hPCP
0.00017
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant F44M ACP substrate from Leishmania major
0.00083
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, wild-type ACP substrate from Leishmania major
0.001
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M/Q48E ACP substrate from Leishmania major
0.0012
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/F44M ACP substrate from Leishmania major
0.0017
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D/Q48E ACP substrate from Leishmania major
0.0038
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, mutant N35D ACP substrate from Leishmania major
0.0082
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli mutant M44F ACP substrate
0.0103
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Mycobacterium tuberculosis
0.014
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, Escherichia coli ACP substrate
0.0192
apo-[acyl-carrier protein]
pH 8.0, 37°C, recombinant His-tagged enzyme, ACP substrate from Plasmodium falciparum
0.183
apo-[peptidyl carrier protein]
pH 8.0, 37°C, substrate BlmI
1.43
apo-[peptidyl carrier protein]
pH 8.0, 37°C, substrate TcmM
0.075
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
additional information
additional information
-
turnover numbers with mutants of peptidyl-carrier protein as substrate
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.054
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37°C, E. coli ACP
0.0006
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37°C, E. coli ACP
0.00042
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.00053
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0024
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.003
6-nitroso-1,2-benzopyrone
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.003
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0052
6-nitroso-1,2-benzopyrone
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0021
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
Bacillus subtilis
-
IC50: 0.0021 mM
0.015
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.015 mM
0.0015
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0015 mM
0.0034
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0034 mM
0.002
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.002 mM
0.00013
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00013 mM
0.0011
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0011 mM
0.0019
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0019 mM
0.0013
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0013 mM
0.00027
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00027 mM
0.0044
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0044 mM
0.00083
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00083 mM
0.03
Bay 11-7085
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.0074
2'-deoxy-adenosine-3',5'-bisphosphate
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.0085
2'-deoxy-adenosine-3',5'-bisphosphate
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.0021
6-nitroso-1,2-benzopyrone
Bacillus subtilis
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0037
6-nitroso-1,2-benzopyrone
Pseudomonas putida
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.004
6-nitroso-1,2-benzopyrone
Pseudomonas aeruginosa
-
in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0091
6-nitroso-1,2-benzopyrone
Bacillus subtilis
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0098
6-nitroso-1,2-benzopyrone
Pseudomonas putida
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.0108
6-nitroso-1,2-benzopyrone
Pseudomonas aeruginosa
-
in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C
0.017
6-nitroso-benzopyrone
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.024
6-nitroso-benzopyrone
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.00078
adenosine-3',5'-bisphosphate
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.0016
adenosine-3',5'-bisphosphate
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.002
Calmidazolium
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.0049
Calmidazolium
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.0011
CoA
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.0047
CoA
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.012
guanidinyl-naltrindole
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.019
guanidinyl-naltrindole
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.0071
PD 404182
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.019
PD 404182
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.0049
sanguinarine
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
0.022
sanguinarine
Mycobacterium tuberculosis
with substrate VibB, recombinant enzyme, pH and temperature not specified in the publication
0.0005
SCH-202676
Mycobacterium tuberculosis
with substrate MAS, recombinant enzyme, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.32
0.32
-
recombinant apo-enzyme, expressed in Escherichia coli DH5alpha
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
less than 20% of maximum activity at both pH 5.0 and 7.0, 50% of activity maximum at pH 5.5 and pH 6.8
5 - 7
-
pH 5: less than 27% of maximal activity, pH 7: less than 62% of maximal activity, activity with apo-[acyl-carrier protein]
6 - 11
-
about 20% of activity maximum at pH 6.5, about 30% of activity maximum at pH 11.0
additional information
the MtAcpS enzyme protein undergoes conformational changes at pHs below pH 6.5, with results in decreases in AcpS activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.25
-
calculated from molar extinction coefficient by the method of Gill and von Hippel
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptomyces pneumoniae
isolated from Yunnan, China
UniProt
brenda
isolated from Yunnan, China
UniProt
brenda
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
brenda
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
brenda
Streptomyces pneumoniae
apcS gene, open reading frame starting at the second Met codon
SwissProt
brenda
strain Gv29-8, gene TRIVIDRAFT_194983; i.e. Hypocrea virens
UniProt
brenda
strain Gv29-8, gene TRIVIDRAFT_48659; i.e. Hypocrea virens
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the mitochondrial localization of the AT3G11470-encoded proteins is validated by the ability of their N-terminal 80-residue leader sequence to guide a chimeric GFP protein to this organelle
brenda
isoenzyme, mutational loss of mitochondrial ACP has no effect on bulk cellular fatty acid synthesis
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily
evolution
-
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
-
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
Q74V64
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. Pseudomonas aeruginosa contains one Sfp-type PPTase, PaPcpS or PcpS with broad substrate specificity, but no AcpS-type PPTase
evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
evolution
phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain. The toxin found in a hybrid PKS-NRPS cluster, (also known as PKS island) produces colibactin. Within this cluster, clbA is identified as a PPTase
evolution
phylogenetic analyses of plant PPT/PPT-like homologues, overview
evolution
PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively
evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
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evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
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evolution
Serratia marcescens Db11
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
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evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
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evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. Pseudomonas aeruginosa contains one Sfp-type PPTase, PaPcpS or PcpS with broad substrate specificity, but no AcpS-type PPTase
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evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
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evolution
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phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases
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evolution
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BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily
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evolution
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PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively
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malfunction
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after 18 h incubation at 37°C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
malfunction
deletion of PPT1 generates mutants that are auxotrophic for lysine, unable to synthesize melanin, hypersensitive to iron and oxidative stress (H2O2) and significantly reduced in virulence to barley cultivar Bowman
malfunction
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deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
malfunction
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enzyme silencing by small interfering RNA in A-549 cells prevents FDH modification. Enzyme-silenced cells demonstrate significantly reduced proliferation and undergo strong G1 arrest
malfunction
inactivation of the enzyme abolishes production of natamycin but not the spore pigment
malfunction
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The ppt1 deletion mutants are auxotrophic for lysine, produce nonpigmented conidia, and are unable to synthesize nonribosomal peptides. Although spore germination is severely compromised under both low and high iron availability, mycelial growth occurs faster than the wild type, and the mutants are able to efficiently colonize plant roots. The ppt1 deletion mutants are unable of inhibiting growth of phytopathogenic fungi in vitro and are defective in induction of salicylic acid-dependent defense responses in Arabidopsis thaliana
malfunction
a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo
malfunction
a T-DNA-tagged null mutant mtppt-1 allele shows an embryo-lethal phenotype. Arabidopsis thaliana RNAi transgenic lines with reduced mtPPT expression display typical phenotypes associated with a deficiency in the mtFAS system, namely miniaturized plant morphology, slow growth, reduced lipoylation of mitochondrial proteins, and the hyperaccumulation of photorespiratory intermediates, glycine and glycolate. the seeds in the mtppt-1 mutant plants failed to develop normally. These morphological and metabolic alterations are reversed when these plants are grown in a non-photorespiratory condition (i.e. 1% CO2 atmosphere), because they are a consequence of a deficiency in photorespiration due to the reduced lipoylation of the photorespiratory glycine decarboxylase. Phenotypes, detailed overview
malfunction
a VabD knockout strain shows no retarded growth under iron-rich conditions, but reduced growth under iron-depletion
malfunction
a xabA knockout strain does not produce albicidin, but when EntD is engineered into the mutant strain, production is restored to wild-type levels
malfunction
gene entD knockout in Escherichia coli strain AN90-60 results in a strain that does not produce enterobactin. Overproduction of AcpS cannot compensate the absence of EntD. Conversely, overexpressing entD on an inducible plasmid cannot complement the absence of acpS. The pobA gene from Burkholderia cenocepacia is shown to efficiently complement an Escherichia coli entD mutant
malfunction
growth defect due to depletion of AcpS. A conditional acpS mutant of AcpS does not catalyze the maturation of IacP, a homologue of acyl carrier proteins. IacP does not complement the lethal phenotype associated with ACP defect in Escherichia coli strain strain EB337
malfunction
inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19
malfunction
inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19, and overexpression of FKPPT3 increases the FK506 production
malfunction
mutants of PswP are unable to produce pigment or surfactant but are still able to produce 2-methyl-3-n-amyl-pyrrole (MAP) and condense it with supplied 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to form prodigiosin. Althiomycin production is eliminated upon deletion of one PPTase gene, SMA2452, whereas the other PPTase gene mutation, SMA4147, has no effect
malfunction
overproduction of AcpS cannot compensate the absence of EntD. Conversely, overexpressing entD on an inducible plasmid cannot complement the absence of acpS
malfunction
Q9UVK7
pleiomorphic phenomena of npgA1 mutant, phenotype, overview
malfunction
the enzyme mutant plants produce no elicitor hydrocarbon terpenes and are not protected against necrotrophic pathogen Botrytis cinerea
malfunction
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pleiomorphic phenomena of npgA1 mutant, phenotype, overview
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malfunction
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a xabA knockout strain does not produce albicidin, but when EntD is engineered into the mutant strain, production is restored to wild-type levels
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malfunction
Serratia marcescens Db11
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mutants of PswP are unable to produce pigment or surfactant but are still able to produce 2-methyl-3-n-amyl-pyrrole (MAP) and condense it with supplied 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to form prodigiosin. Althiomycin production is eliminated upon deletion of one PPTase gene, SMA2452, whereas the other PPTase gene mutation, SMA4147, has no effect
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malfunction
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a VabD knockout strain shows no retarded growth under iron-rich conditions, but reduced growth under iron-depletion
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malfunction
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a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo
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malfunction
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inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19
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malfunction
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inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19, and overexpression of FKPPT3 increases the FK506 production
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malfunction
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inactivation of the enzyme abolishes production of natamycin but not the spore pigment
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malfunction
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after 18 h incubation at 37°C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
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malfunction
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deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
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metabolism
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AcpS is a doubly promiscuous enzyme capable of activation of acyl-carrier proteins from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates
metabolism
isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal
metabolism
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isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
metabolism
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isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
metabolism
isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
metabolism
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the enzyme is essential for activation of non-ribosomal peptide synthetase and polyketide synthase enzymes
metabolism
the demonstration that ACP homologue IacP is matured by AcpS establishes a cross-connection between virulence and fatty acid biosynthesis pathways
metabolism
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isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
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metabolism
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isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal
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metabolism
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isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
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metabolism
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isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
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physiological function
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isoform PPT1 in plays an important role antibiosis and induction of salicylic acid and camalexin-dependent plant defense responses
physiological function
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isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
physiological function
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment
physiological function
Sfp-type 4-phosphopantetheinyl transferase is required for lysine synthesis, tolerance to oxidative stress and virulence of Cochliobolus sativus on barley cultivar Bowman. Isoform PPT1 is involved in conidiation, but does not affect the size, morphology and germination of conidia
physiological function
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the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
physiological function
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors
physiological function
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors
physiological function
phosphopantetheinyl transferase activates biosynthetic pathways that synthesize both primary and secondary metabolites in bacteria
physiological function
phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations
physiological function
phosphopantetheinyl transferases play an essential role in the biosyntheses of fatty acids, polyketides, and nonribosomal peptides
physiological function
PPTase AcpS is essential in Salmonella. Acyl carrier proteins are mainly involved in fatty acid biosynthesis, and they require posttranslational maturation by addition of a 4'-phosphopantetheine prosthetic group to be functional, analysis of SPI-1 or IacP, a homologue of acyl carrier proteins, maturation in vivo, overview. Although IacP is similar to ACP and matured by using the same enzyme, IacP cannot replace the essential function of ACP in fatty acid synthesis
physiological function
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. AcpSs are primarily used for post-translational modification and activation of the carrier proteins of FASs (primary metabolism) across a diversity of organisms making them the most commonly found PPTase
physiological function
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis
physiological function
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis
physiological function
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PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. Enzyme Gsp plays a role in gramicidin S biosynthesis
physiological function
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. The PPTase ClbA can activate both siderophore and genotoxin biosynthesis
physiological function
some Vibrio anguillarum strains produce the siderophore vanchrobactin utilizing the NRPS VabF. VabD is the dedicated PPTase used for 4'-phosphopantetheinylation of VabF. Vibrio anguillarum strains also contain a second, more dominant, siderophore anguibactin, located on the pJM1 plasmid. Anguibactin is also synthesized by an NRPS and requires the PPTase AngD. Both VabD and AngD can complement one another, but since anguibactin is the more potent siderophore, some strains have lost the vanchrobactin biosynthesis pathway
physiological function
Streptomyces coelicolor contains 25 biosynthetic secondary metabolite clusters that produce natural products, including actinorhodin, coelichelin, coelibactin, TW95a, EPA, methylenomycin (encoded on a giant linear plasmid), prodiginines and the antibiotic CDA. All of these natural products are produced by synthases that require phoshopantetheinylation by an AcpS-type PPTase, which shows a high level of permissiveness for CoA substrates as well as carrier proteins. For example, type I mammalian FAS, type I fungal PKS, and several type II bacterial ACPs are efficiently phosphopantetheinylated. The genome of Streptomyces coelicolor contains two other PPTases: RedU, which is a dedicated PPTase for undecylprodigiosin biosynthesis, and SCO6673 required for CDA biosynthesis. Both RedU and SCO6673 have specific carrier protein targets, whereas ScAcpS shows broad activity. The crystal structure of ScAcpS shows the structural basis for relaxed substrate selection
physiological function
Streptomyces coelicolor contains 25 biosynthetic secondary metabolite clusters that produce natural products, including actinorhodin, coelichelin, coelibactin, TW95a, EPA, methylenomycin (encoded on a giant linear plasmid), prodiginines and the antibiotic CDA. All of these natural products are produced by synthases that require phoshopantetheinylation by an AcpS-type PPTase, which shows a high level of permissiveness for CoA substrates as well as carrier proteins. For example, type I mammalian FAS, type I fungal PKS, and several type II bacterial ACPs are efficiently phosphopantetheinylated. The genome of Streptomyces coelicolor contains two other PPTases: RedU, which is a dedicated PPTase for undecylprodigiosin biosynthesis, and SCO6673 required for CDA biosynthesis. Both RedU and SCO6673 have specific carrier protein targets, whereas ScAcpS shows broad activity. The crystal structure of ScAcpS shows the structural basis for relaxed substrate selection. In Streptomyces coelicolor, which also produces prodiginine, the PPTase RedU is responsible for 4'-phosphopantetheinylation of RedO but not for the other PCP and ACP domains
physiological function
The 4'-phosphopantetheine (4'PPT) portion of coenzyme A (CoA) is an essential group for many carrier proteins and enzymes. Addition of this group is required for the correct function of polyketide synthase (PKS), non-ribosomal peptide synthetase and fatty acid synthase. The 4'PPT group is transferred to a highly conserved serine motif in the acceptor protein in a magnesium dependent reaction by phosphopantetheinyl transferases (PPTases). Gene PPT2 encoding a phosphopantetheinyl transferase and is essential for growth in Candida albicans
physiological function
the biosyntheses of the red pigment prodigiosin and the surfactant serrawettin W1 in Serratia marcescens depend on the presence of the PPTase PswP. Serratia species appear to employ two PPTases, one to activate the PCP of PigG and one to activate the ACPs of PigH. Besides PswP, PigL also is a PPTase. Two Sfp/EntD-type PPTases are identified, encoded by genes SMA4147 and SMA2452
physiological function
Q9UVK7
the enzyme is essential for growth, and for formation of conidia and cleistothecium in development
physiological function
the enzyme is essential for the viability of the bacterium
physiological function
the enzyme is essential. Two siderophores, pyoverdin and pyochelin, are produced by NRPSs and associated with the virulence of these bacteria. Pyoverdine biosynthesis requires phoshopantetheinylation of PvdD, PvdI and PvdJ and pyochelin biosynthesis requires activation of PchE and PchF. PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins, but the PPTase is optimized for primary metabolism, since its activity drops 30-fold for ACPs or PCPs from secondary metabolism in vitro
physiological function
the enzyme PptT is the PPTase for the mycobactin synthase. Siderophores in Mycobacterium tuberculosis are peptide-based and fall into two categories, the water-soluble exochelins and the membrane-associated mycobactins. siderophore or other natural product production is regulated by the activity of the PPTase. PptT is necessary for in vitro growth of mycobacteria, but mycobacteria require enzymes in vitro that are not always required in vivo. PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. AcpSs are primarily used for post-translational modification and activation of the carrier proteins of FASs (primary metabolism) across a diversity of organisms making them the most commonly found PPTase. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
physiological function
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS). A crucial role of mtPPT for embryogenesis. MtPPT contributes to mtFAS and photorespiration
physiological function
the PobA PPTase efficiently functionally complements an Escherichia coli entD mutant
physiological function
the PPTase XabA is essential for albicidin production
physiological function
Trichoderma virens volatile organic compounds elicit both development and defense programs and enzyme PPT1 plays an important role in biosynthesis of terpenes (including the sesquiterpenes beta-caryophyllene, (-)-beta-elemene, germacrene D, Tau-cadinene, delta-cadinene, alpha-amorphene, and Tau-selinene and the monoterpenes beta-myrcene, trans-beta-ocimene, and cis-beta-ocimene) and plant protection against Botrytis cinerea, overview
physiological function
Vibrio cholerae is a bacterial pathogen that biosynthesizes a unique siderophore, vibriobactin, using biosynthetic machinery similar to enterobactin synthase. Both VibB and VibF are phosphopantetheinylated by the PPTase VibD
physiological function
Pseudomonas aeruginosa acyl carrier proteins, AcpP1, AcpP2, and AcpP3, are successfully phosphopantetheinylated by PcpS, while only AcpP1 can be used as a substrate for the synthesis of fatty acids in cell free extracts in vitro
physiological function
-
the enzyme is essential for growth, and for formation of conidia and cleistothecium in development
-
physiological function
-
PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis
-
physiological function
-
the PPTase XabA is essential for albicidin production
-
physiological function
-
the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
-
physiological function
Serratia marcescens Db11
-
the biosyntheses of the red pigment prodigiosin and the surfactant serrawettin W1 in Serratia marcescens depend on the presence of the PPTase PswP. Serratia species appear to employ two PPTases, one to activate the PCP of PigG and one to activate the ACPs of PigH. Besides PswP, PigL also is a PPTase. Two Sfp/EntD-type PPTases are identified, encoded by genes SMA4147 and SMA2452
-
physiological function
-
some Vibrio anguillarum strains produce the siderophore vanchrobactin utilizing the NRPS VabF. VabD is the dedicated PPTase used for 4'-phosphopantetheinylation of VabF. Vibrio anguillarum strains also contain a second, more dominant, siderophore anguibactin, located on the pJM1 plasmid. Anguibactin is also synthesized by an NRPS and requires the PPTase AngD. Both VabD and AngD can complement one another, but since anguibactin is the more potent siderophore, some strains have lost the vanchrobactin biosynthesis pathway
-
physiological function
-
the enzyme is essential. Two siderophores, pyoverdin and pyochelin, are produced by NRPSs and associated with the virulence of these bacteria. Pyoverdine biosynthesis requires phoshopantetheinylation of PvdD, PvdI and PvdJ and pyochelin biosynthesis requires activation of PchE and PchF. PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins, but the PPTase is optimized for primary metabolism, since its activity drops 30-fold for ACPs or PCPs from secondary metabolism in vitro
-
physiological function
-
Streptomyces coelicolor contains 25 biosynthetic secondary metabolite clusters that produce natural products, including actinorhodin, coelichelin, coelibactin, TW95a, EPA, methylenomycin (encoded on a giant linear plasmid), prodiginines and the antibiotic CDA. All of these natural products are produced by synthases that require phoshopantetheinylation by an AcpS-type PPTase, which shows a high level of permissiveness for CoA substrates as well as carrier proteins. For example, type I mammalian FAS, type I fungal PKS, and several type II bacterial ACPs are efficiently phosphopantetheinylated. The genome of Streptomyces coelicolor contains two other PPTases: RedU, which is a dedicated PPTase for undecylprodigiosin biosynthesis, and SCO6673 required for CDA biosynthesis. Both RedU and SCO6673 have specific carrier protein targets, whereas ScAcpS shows broad activity. The crystal structure of ScAcpS shows the structural basis for relaxed substrate selection
-
physiological function
-
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors
-
physiological function
-
the enzyme PptT is the PPTase for the mycobactin synthase. Siderophores in Mycobacterium tuberculosis are peptide-based and fall into two categories, the water-soluble exochelins and the membrane-associated mycobactins. siderophore or other natural product production is regulated by the activity of the PPTase. PptT is necessary for in vitro growth of mycobacteria, but mycobacteria require enzymes in vitro that are not always required in vivo. PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. AcpSs are primarily used for post-translational modification and activation of the carrier proteins of FASs (primary metabolism) across a diversity of organisms making them the most commonly found PPTase. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis
-
physiological function
-
the enzyme is essential for the viability of the bacterium
-
physiological function
-
phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations
-
physiological function
-
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment
-
physiological function
-
phosphopantetheinyl transferases play an essential role in the biosyntheses of fatty acids, polyketides, and nonribosomal peptides
-
physiological function
-
isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
-
additional information
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, catalytic mechanism of PptT, overview. While important for CoA binding, Arg48 and Arg56 likely play very small roles in catalysis
additional information
-
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, catalytic mechanism of PptT, overview. While important for CoA binding, Arg48 and Arg56 likely play very small roles in catalysis
additional information
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, overview
additional information
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts
additional information
Q9UVK7
loss-of-function of LYS5 mutant DNPG, which encodes a PPTase in Saccharomyces cerevisiae strain BY4741, is functionally complemented by NpgA, and Escherichia coli-derived NpgA reveals phosphopantetheinylation activity with the elaboration of 3'5'-ADP
additional information
-
loss-of-function of LYS5 mutant DNPG, which encodes a PPTase in Saccharomyces cerevisiae strain BY4741, is functionally complemented by NpgA, and Escherichia coli-derived NpgA reveals phosphopantetheinylation activity with the elaboration of 3'5'-ADP
additional information
the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule
additional information
-
the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule
additional information
-
loss-of-function of LYS5 mutant DNPG, which encodes a PPTase in Saccharomyces cerevisiae strain BY4741, is functionally complemented by NpgA, and Escherichia coli-derived NpgA reveals phosphopantetheinylation activity with the elaboration of 3'5'-ADP
-
additional information
-
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, catalytic mechanism of PptT, overview. While important for CoA binding, Arg48 and Arg56 likely play very small roles in catalysis
-
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts
-
additional information
-
the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule
-
Show AA Sequence and Transmembrane Helices (29319 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13390
15000
18470
-
2 * 18470, calculated from molar extinction coefficient by the method of Gill and von Hippel
20000
x * 20000, isoform AcpS, calculated from amino acid sequence
20320
mitochondrial isoenzyme, calculated from open reading frame
27000
28000
29000
34000
41000
Streptomyces pneumoniae
AcpS, native homotrimer, predicted from nucleotide sequence
34000
x * 34000, isoform Sfp, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotrimer
monomer
trimer
additional information
?
x * 20000, isoform AcpS, calculated from amino acid sequence
?
x * 34000, isoform Sfp, calculated from amino acid sequence
homodimer
Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance
homodimer
-
Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance
-
homodimer
-
Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance
homodimer
-
2 * 18470, calculated from molar extinction coefficient by the method of Gill and von Hippel
homodimer
Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance
homotrimer
3 * 28000, AcpS has a quaternary structure with active sites shared across each homotypic interface
homotrimer
3 * 28000, AcpS has a quaternary structure with active sites shared across each homotypic interface
homotrimer
-
3 * 28000, AcpS has a quaternary structure with active sites shared across each homotypic interface
-
additional information
the protein structure model fuses an N-terminal COP1 interacting protein domain with a C-terminal Sfp-like PPT domain. The PPT domain of the predicted AT2G02770 protein shares 73% similarity and 67% identity with the mtPPT protein encoded by splicing variant AT3G11470.1
additional information
the protein structure model fuses an N-terminal COP1 interacting protein domain with a C-terminal Sfp-like PPT domain. The PPT domain of the predicted AT2G02770 protein shares 73% similarity and 67% identity with the mtPPT protein encoded by splicing variant AT3G11470.1
additional information
Q9UVK7
enzyme NpgA contains a PPTase superfamily domain, which has a conserved sequence of (V/I)G(V/I)DX(78)(F/W)(S/C/T)XKE(A/S)hhK sequence between aa 187-277, similar to PPTases of other organisms
additional information
-
enzyme NpgA contains a PPTase superfamily domain, which has a conserved sequence of (V/I)G(V/I)DX(78)(F/W)(S/C/T)XKE(A/S)hhK sequence between aa 187-277, similar to PPTases of other organisms
additional information
-
enzyme NpgA contains a PPTase superfamily domain, which has a conserved sequence of (V/I)G(V/I)DX(78)(F/W)(S/C/T)XKE(A/S)hhK sequence between aa 187-277, similar to PPTases of other organisms
-
additional information
enzyme PptT possesses a pseudodimeric fold characteristic of Sfp-type PPTases, three-dimensional structure comparisons, modeling, overview
additional information
-
enzyme PptT possesses a pseudodimeric fold characteristic of Sfp-type PPTases, three-dimensional structure comparisons, modeling, overview
additional information
Mycobacterium tuberculosis type-II PPTase PptT reveals an alpha/beta fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry
additional information
-
Mycobacterium tuberculosis type-II PPTase PptT reveals an alpha/beta fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry
additional information
-
Mycobacterium tuberculosis type-II PPTase PptT reveals an alpha/beta fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry
-
additional information
-
enzyme PptT possesses a pseudodimeric fold characteristic of Sfp-type PPTases, three-dimensional structure comparisons, modeling, overview
-
additional information
enzyme MuPPT possesses a pseudodimeric fold characteristic of Sfp-type PPTases, three-dimensional structure comparisons, modeling, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of ACPS in unliganded and holo-ACPP-bound forms, to 2.05 A and 4.10 A resolution, respectively. ACPS binds three product holo-ACPP molecules to form a 3:3 hexamer. The binding interface is organized to arrange contacts between positively charged ACPS residues and the holo-ACPP phosphopantetheine moiety
apo-PPT (PDB: 2BYD) or in complex with coenzyme A (CoA, 5 mM) and Mg2+ (20 mM) (PDB: 2C43) or coenzyme A (2.5 mM) and acyl-carrier protein (S2156A mutant of ACP domain of fatty acid synthase) (PDB: 2CG5), precipitant: 14% PEG3350 and 0.05 M H3Cit/Na3Cit pH 5.7 or 2 M NaCl and 10% PEG6000 (complexes), apo-PPT: space group: P2(1)2(1)2(1), unit cell parameters: a: 63.78, b: 69.95, c: 71.24, alpha/beta fold with pseudo 2fold symmetry, N-terminal beta sheet (residues 91-116) connected to C-terminal beta sheet (residues 207-239) by a one residue linker and unique N-terminal and C-terminal extensions of 13 and 52 amino acids, respectively, PPT-CoA complex: space group: P2(1)2(1)2(1), unit cell parameters: a: 65.59, b: 68.96, c: 70.75, CoA-binding at the interface of N- and C-terminal domain mediated by PPT residues 47, 86, 110, 111, 185 (hydrophobic interactions, hydrogen bonds and salt bridges), and independent of Mg2+, Mg2+ bound through PPT residues 181 and 129 and coordinated by a water molecule, PPT-CoA-ACP complex: space group: P3(2)21, unit cell parameters: a, b: 69.36, c: 184.7, ACP-binding in the cleft between N- and C-terminal domain causes their rotation and slight closure, and is facilitated predominantly by hydrophobic interactions with PPT residues 51-54, 191, 144-148, 173, and 177 and a few polar interactions, disorder of C-terminal coil (residues 290-305), lack of Mg2+
crystallized by vapour-diffusion method, crystals belong to space group R3, with unit cell parameters a = b = 68.53, c = 85.9 A
-
purified recombinant MBP-fusion enzyme, X-ray diffraction structure determination and analysis at 1.59 A resolution
purified recombinant MBP-tagged type-II PPTase PptT, hanging drop vapor diffusion, mixing of 0.002 ml of 10 mg/ml protein in 20 mM MES, pH 6.7, 300 mM NaCl, 10% v/v glycerol, 0.5 mM tris(2-carboxyethyl)phosphine, and 1 mM CoA, with 0.001 ml of reservoir solution containing 1.6 M sodium citrate, 18°C, method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution, modeling. No crystals can be grown without added CoA. Recombinantly expressed enzyme PptT as N- or C-terminally His6-tagged proteins are soluble protein in Escherichia coli, but both are unstable over time and neither can be crystallized
purified recombinant MBP-fusion enzyme, X-ray diffraction structure determination and analysis at 1.65 A resolution
complexed with CoA and acetyl-CoA, and mutant enzymes H110A and D111A, vapor diffusion method. Crystals of the AcpS-CoA-Mg2+ complex are obtained at 18°C, from 0.3 M potassium thiocyanate (KSCN), 0.1 M sodium cacodylate (NaCac) (pH 6.5), and 15% (w/v) PEG 4000. The best diffracting crystal of the AcpS-acetyl-CoA complex is obtained in 0.2 M lithium sulfate, 25% (w/v) PEG 2000 MME, and 0.1 M NaCac (pH 6.5), in the presence of 5 mM acetyl-CoA. The D111A mutant crystallizes in 0.2 M KSCN, 0.1 M NaCac (pH 6.5), 8% (w/v) PEG 20000, and 8% (w/v) PEG 550 MME. The H110A mutant crystal is obtained in 0.3 Ms odium acetate, 0.1 M NaCac (pH 6.5), and 25% (w/v) PEG 2000 MME
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D107A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D107E
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
E151A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105D
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
K155A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
K44A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
R14A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
W147A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
W147F
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D129A
reduced Mg2+ affinity and catalytic efficiency, D129 plays a role in Mg2+-coordination
E181A
significant loss in enzyme activity, reduced Mg2+ affinity and catalytic efficiency
E181Q
significant loss in enzyme activity, reduced Mg2+ affinity (20fold) and catalytic efficiency (300fold)
Q112E, E181Q
double mutant, reduced Mg2+ affinity (200fold) and catalytic efficiency
D114N
site-directed mutagenesis, the mutation eliminates the negative charge of one of the putative Mg2+ ligands, also abolishes phosphopantetheinylation activity of PptT, inactive mutant
E109D
site-directed mutagenesis, inactive mutant, no measurable catalytic activity
E116Q
site-directed mutagenesis, the mutant shows 500fold reduced activity compared to the wild-type enzyme
E157Q
site-directed mutagenesis, removal of the negative charge associated with the putative Mg2+ ligand/general base abolishes phosphopantetheinylation activity, inactive mutant
R48A
site-directed mutagenesis, the mutation disrupts 3'-phosphate binding, the activity is reduced by 20fold compared to the wild-type enzyme
R56A
site-directed mutagenesis, the mutation disrupts 3'-phosphate binding, the activity is reduced by 100fold compared to the wild-type enzyme
E109D
-
site-directed mutagenesis, inactive mutant, no measurable catalytic activity
-
E116Q
-
site-directed mutagenesis, the mutant shows 500fold reduced activity compared to the wild-type enzyme
-
E157Q
-
site-directed mutagenesis, removal of the negative charge associated with the putative Mg2+ ligand/general base abolishes phosphopantetheinylation activity, inactive mutant
-
R48A
-
site-directed mutagenesis, the mutation disrupts 3'-phosphate binding, the activity is reduced by 20fold compared to the wild-type enzyme
-
R56A
-
site-directed mutagenesis, the mutation disrupts 3'-phosphate binding, the activity is reduced by 100fold compared to the wild-type enzyme
-
additional information
additional information
a T-DNA-tagged mutant allele (SALK_152625C) of AT2G02770 was identified in which the insertion resides in the COP1 interacting protein domain
additional information
a T-DNA-tagged mutant allele (SALK_152625C) of AT2G02770 was identified in which the insertion resides in the COP1 interacting protein domain
additional information
generation of mtPPT enzyme mutant plants, phenotype, overview
additional information
generation of mtPPT enzyme mutant plants, phenotype, overview
additional information
Q9UVK7
generation of a npgA knockout mutant in strain SNT611
additional information
-
generation of a npgA knockout mutant in strain SNT611
additional information
-
generation of a npgA knockout mutant in strain SNT611
-
additional information
cloning of PPT2 promoter replacement construct and a deletion construct from strain SN76, by placing one allele under the control of the regulatable MET3 promoter, and deleting the remaining allele. Phenotypes of the heterozygous and the conditional null mutant, overview
additional information
-
cloning of PPT2 promoter replacement construct and a deletion construct from strain SN76, by placing one allele under the control of the regulatable MET3 promoter, and deleting the remaining allele. Phenotypes of the heterozygous and the conditional null mutant, overview
additional information
-
isoform AcpT cannot functially replace isoform AcpS. However, in the absence of AcpS activity, isoform AcpT allows very slow growth
additional information
construction of a conditional pptT mutant in Mycobacterium tuberculosis strain H37Rv showing retarded growth and persistence. Construction of mutants in which the PPTase gene is controlled by a tetracycline promoter, for conditional regulation of the PptT expression
additional information
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts. In vivo, the highest fluorescence levels is attained for the full-length enzyme and N-terminally truncated variants whereas truncation of the last C-terminal residue L227 is sufficient to negatively impact the fluorescence intensity of the colonies
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts. In vivo, the highest fluorescence levels is attained for the full-length enzyme and N-terminally truncated variants whereas truncation of the last C-terminal residue L227 is sufficient to negatively impact the fluorescence intensity of the colonies
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts. In vivo, the highest fluorescence levels is attained for the full-length enzyme and N-terminally truncated variants whereas truncation of the last C-terminal residue L227 is sufficient to negatively impact the fluorescence intensity of the colonies
-
additional information
-
construction of a conditional pptT mutant in Mycobacterium tuberculosis strain H37Rv showing retarded growth and persistence. Construction of mutants in which the PPTase gene is controlled by a tetracycline promoter, for conditional regulation of the PptT expression
-
additional information
creation of an conditionally inactive acpS mutant
additional information
-
creation of an conditionally inactive acpS mutant
additional information
enzyme inactivation mutant shows 93% reduction in fredericamycin synthesis
additional information
-
enzyme inactivation mutant shows 93% reduction in fredericamycin synthesis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite heat labile, unstable during chromatographic procedures intended for its purification, can only be partially overcome by Mg2+ and dithiothreitol, addition of ethylene glycol, glycerol, EDTA or proteinase inhibitors failed to stabilize the plant enzyme
-
very unstable, markedly protected from inactivation by the presence of half-saturating concentrations of reduced CoA
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, stored in liquid nitrogen, enzyme maintains full activity for at least 1 year
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from bacterial lysate by immobilized metal affinity chromatography followed by gel filtration chromatography on Superdex200 HiLoad 26/60 column and concentration to 20 mg/ml or anion exchange chromatography and dialysis
Ni-NTA column chromatography
partially
recombinant enzyme
recombinant enzyme, expressed in Escherichia coli
recombinant His-tagged enzyme from Bacillus subtilis from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged wild-type full-length PptT and N- and C-terminally truncated mutant enzymes from Escherichia coli strain BL21(DE3) and recombinant soluble MBP-fusion PptT by immobilized metal ion affinity chromatography and gel filtration. The MBP-tagged enzyme irreversibly precipitates after proteolytic cleavage of the N-terminal MBP tag
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Q9UVK7
recombinant MBP-fusion enzyme
recombinant MBP-tagged type II PPTase PptT from Escherichia coli strain BL21(DE3) amylose affinity chromatography, anion exchange chromatography, and gel filtration
recombinant N-terminaly His6-tagged enzyme from Escherichia coli BL21(DE3) by nickel affinity chromatography
recombinant tagged isozyme from Escherichia coli by affinity chromatography
recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by immobilized metal affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
acpP gene amplified from a genomic Vibrio harveyi library by PCR, cloned and transformed in to Escherichia coli Bl-21
cloned in Escherichia coli DH5alpha and overexpressed in Escherichia coli MV1190/pUC8-Sfp
-
CpSFP-PPT is expressed from an artificially synthesized gene with codon usage optimized for Escherichia coli
DNA and amino acid sequence determination and analysis, recombinant expression of tagged isozyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
gene AASDHPPT, recombinant expression of the Sfp-PPTase from plasmid pET29b in Escherichia coli strain BL21(DE3)
gene acpP cloned and overproduced from recombinant Escherichia coli BL21(DE3)pDPJ
-
gene acpS, DNA and amino acid sequence determination and analysis, recombinant expression of tagged isozyme in Escherichia coli
gene acpS, recombinant expression of N-terminaly His6-tagged enzyme in Escherichia coli BL21(DE3) from plasmid pHJ0024
gene AT2G02770, a pseudogene, DNA and amino acid sequence determination and analysis, gene modeling
gene AT3G11470, encoding the mitchondrial isozyme, has three splicing variants AT3G11470.1, AT3G11470.2, and AT3G11470.3, which are the result of alternative slicing that occurs in removing the second intron, DNA and amino acid sequence determination and analysis. The AT3G11470.3 protein is inactive. Quantitative RT-PCR expression analysis
gene BSU03570, recombinant expression of His-tagged enzyme from Bacillus subtilis in Escherichia coli
gene clbA, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon
gene entD, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon
gene LMJF_20_0830, recombinant expression of His-tagged enzyme from Leishmania major in Escherichia coli
gene npgA, DNA and amino acid sequence determination and analysis, recombinant overexpression of His6-tagged enzyme in Aspergillus nidulans npgA knockout strain SNT611 using the niiA promoter, and as His6-tagged enzyme in Escherichia coli, functional complementation of Saccharomyces cerevisiae strain BY4741 knockout mutant DPNG
Q9UVK7
gene PPT2, DNA and amino acid sequence determination and analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
gene pptT, recombinant expression of His-tagged wild-type full-length PptT and N- and C-terminally truncated mutant enzymes in Escherichia coli strain BL21(DE3), the wild-type full-lebgth enzyme forms aggregates, expression of the enzyme with a ubiquitin-related modifier tag (SUMO) has no effect on the protein solubility, while fusion with the maltose-binding-protein results in a soluble fusion protein that can be purified
gene Rv2794c or pptT, recombinant expression of MBP-tagged type II PPTase PptT in Escherichia coli strain BL21(DE3)
gene sfp, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon
gene XALc_0101, DNA and amino acid sequence determination and analysis, the Xab gene cluster is expressed on two plasmids in Xanthomonas axonopodis pv. vesicatoria, and showa a 6fold increased yield of the antibiotic albicidin
genes acpS and acpP cloned and overexpressed in Escherichia coli, acpS complements an Escherichia coli mutant
Streptomyces pneumoniae
genes sfp or entD, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon
in pCOEX1 for expression with TEV protease-cleavable N-terminal hexa-His-tag in Escherichia coli BL21(DE3)-R3
mtaA gene of myxothiazol biosyntheic gene cluster, heterlogous coexpression with an acyl carrier protein domain in Escherichia coli XL1blue
open reading frame YPL148C is the potential mitochondrial PPTase gene, expressed in Escherichia coli and Saccharomyces cerevisiae
overexpression as a C-terminal His6-tag fusion protein in Escherichia coli
-
PPTase gene gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
PPtase gene npgA complements the lys5 deletion in Saccharomyces cerevisiae
-
PPtase gene q10474, the putative lys7 gene, complements the lys5 deletion in Saccharomyces cerevisiae
-
PPTase gene Sfp and Gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
recombinant expression of enzyme PptT as maltose-binding-protein fusion protein
region from the rat FAS including putative acyl carrier protein cloned and overexpressed in Escherichia coli strains DH5alpha and BL21(DE3)
-
svp gene cloned into pQE-70 and overproduced in Escherichia coli M15(pREP4)
recombinant expression of enzyme PptT as maltose-binding-protein fusion protein
recombinant expression of enzyme PptT as maltose-binding-protein fusion protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is upregulated during infection of the human host
the enzyme is upregulated during infection of the human host
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
drug development
medicine
molecular biology
synthesis
analysis
-
enzyme can be utilized in an assay for apo-ACP in biological material
analysis
method for the generation of crypto-AcpM loaded with a solvatochromic probe 7-nitrobenz-2-oxa-1,3-diazol-4-yl, which is linked to the 4'-phosphopantetheine (Ppant) prosthetic group of AcpM by Sfp. The crypto-AcpM is employed to explore the elusive dynamics of Ppant arm in AcpM
analysis
-
method for the generation of crypto-AcpM loaded with a solvatochromic probe 7-nitrobenz-2-oxa-1,3-diazol-4-yl, which is linked to the 4'-phosphopantetheine (Ppant) prosthetic group of AcpM by Sfp. The crypto-AcpM is employed to explore the elusive dynamics of Ppant arm in AcpM
-
biotechnology
mutant ACPs will be valuable in dissecting the structure-function relationships of ACP and its participation in synthesis and regulation of fatty acid, phospholipids, and other products of medical and biotechnological importance
biotechnology
-
identification of short peptide tags of 12 residues as efficient substrate for site-specific protein labeling catalyzed by enzyme
biotechnology
-
identification of short peptide tags of 12 residues as efficient substrate for site-specific protein labeling catalyzed by enzyme
biotechnology
biotechnological de novo production of m-cresol from sugar in complex yeast extract-peptone medium with the yeast Saccharomyces cerevisiae. A heterologous pathway based on the decarboxylation of the polyketide 6-methylsalicylic acid is introduced into a CEN.PK yeast strain. Overexpression of codon-optimized 6-methylsalicylic acid synthase from Penicillium patulum together with activating phosphopantetheinyl transferase npgA from Aspergillus nidulans results in up to 367 mg/l 6-methylsalicylic acid production. Additional genomic integration of the genes have a strongly promoting effect and 6-methylsalicylic acid titers reach more than 2 g/l. Simultaneous expression of 6-methylsalicylic acid decarboxylase patG from Aspergillus clavatus leads to the complete conversion of 6-methylsalicylic acid and production of up to 589 mg/L m-cresol
drug development
the enzyme is a broad-spectrum target for design of antifungal drugs
drug development
the human pathogen Mycobacterium tuberculosis PPTases are attractive drug targets
drug development
-
the human pathogen Mycobacterium tuberculosis PPTases are attractive drug targets
-
medicine
producer of the hybrid peptide-polyketide antitumor drug bleomycin
medicine
Streptomyces pneumoniae
-
enzyme plays an important role in bacterial fatty acid and lipid biosynthesis, making it an attractive target for therapeutic intervention, drug design by identifying inhibitors with potential antibacterial activity
medicine
-
producer of the hybrid peptide-polyketide antitumor drug bleomycin
-
molecular biology
MtaA should be a usefool tool for activating heterologously expressed polyketide synthase and nonribosomal polyketide synthase systems
molecular biology
insights in molecular architecture and reaction mechanism of group II PPTs in contrast to group I PPTs (bacterial) enable screening for antibacterial agents which specifically inhibit bacterial PPTs
molecular biology
SchPPT is a promiscuous PPTase and may be used on polyketide production in heterologous bacterial host and labeling of acyl-carrier proteins, ACPs
molecular biology
-
SchPPT is a promiscuous PPTase and may be used on polyketide production in heterologous bacterial host and labeling of acyl-carrier proteins, ACPs
-
synthesis
the broad specificity of the single PPTase present in Pseudomonas can be used to 4'-phosphopantetheinylate various carrier proteins
synthesis
biotechnological de novo production of m-cresol from sugar in complex yeast extract-peptone medium with the yeast Saccharomyces cerevisiae. A heterologous pathway based on the decarboxylation of the polyketide 6-methylsalicylic acid is introduced into a CEN.PK yeast strain. Overexpression of codon-optimized 6-methylsalicylic acid synthase from Penicillium patulum together with activating phosphopantetheinyl transferase npgA from Aspergillus nidulans results in up to 367 mg/l 6-methylsalicylic acid production. Additional genomic integration of the genes have a strongly promoting effect and 6-methylsalicylic acid titers reach more than 2 g/l. Simultaneous expression of 6-methylsalicylic acid decarboxylase patG from Aspergillus clavatus leads to the complete conversion of 6-methylsalicylic acid and production of up to 589 mg/L m-cresol
synthesis
-
the broad specificity of the single PPTase present in Pseudomonas can be used to 4'-phosphopantetheinylate various carrier proteins
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prescott, D.J.; Vagelos, P.R.
Acyl carrier protein
Adv. Enzymol. Relat. Areas Mol. Biol.
36
269-311
1972
Saccharomyces cerevisiae, Clostridium kluyveri, Escherichia coli, Rattus norvegicus
brenda
Elovson, J.; Vagelos, P.R.
Acyl carrier protein. X. Acyl carrier protein synthetase
J. Biol. Chem.
243
3603-3611
1968
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Prescott, D.J.; Elovson, J.; Vagelos, P.R.
Acyl carrier protein synthetase
Methods Enzymol.
35B
95-101
1975
Escherichia coli, Escherichia coli B / ATCC 11303
-
brenda
Werkmeister, K.; Wieland, F.; Schweizer, E.
Coenzyme A: fatty acid synthetase apoenzyme 4-phosphopantetheine transferase in yeast
Biochem. Biophys. Res. Commun.
96
483-490
1980
Saccharomyces cerevisiae
brenda
Elhussein, S.A.; Miernyk, J.A.; Ohlrogge, J.B.
Plant holo-(acyl carrier protein) synthase
Biochem. J.
252
39-45
1988
Ricinus communis, Spinacia oleracea
brenda
Yang, L.M.; Fernandez, M.D.; Lamppa, G.K.
Acyl carrier protein (ACP) import into chloroplasts. Covalent modification by a stromal holoACP synthase is stimulated by exogenously added CoA and inhibited by adenosine 3',5'-bisphosphate
Eur. J. Biochem.
224
743-750
1994
Spinacia oleracea, Spinacia oleracea Melody
brenda
Lambalot, R.H.; Walsh, C.T.
Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase
J. Biol. Chem.
270
24658-24661
1995
Escherichia coli
brenda
Revill, W.P.; Bibb, M.J.; Hopwood, D.A.
Relationships between fatty acid and polyketide synthases from Streptomyces coelicolor A3(2): characterization of the fatty acid synthase acyl carrier protein
J. Bacteriol.
178
5660-5667
1996
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
brenda
Gehring, A.M.; Lambalot, R.H.; Vogel, K.W.; Drueckhammer, D.G.; Walsh, C.T.
Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase
Chem. Biol.
4
17-24
1997
Escherichia coli
brenda
Lambalot, R.H.; Walsh, C.T.
Holo-[acyl-carrier-protein] synthase of Escherichia coli
Methods Enzymol.
279
254-262
1997
Escherichia coli
brenda
Stuible, H.P.; Meier, S.; Schweizer, E.
Identification, isolation and biochemical characterization of a phosphopantetheine:protein transferase that activates the two type-I fatty acid synthases of Brevibacterium ammoniagenes
Eur. J. Biochem.
248
481-487
1997
Corynebacterium ammoniagenes
brenda
Quadri, L.E.; Weinreb, P.H.; Lei, M.; Nakano, M.M.; Zuber, P.; Walsh, C.T.
Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
Biochemistry
37
1585-1595
1998
Bacillus subtilis
brenda
Stuible, H.P.; Meier, S.; Wagner, C.; Hannappel, E.; Schweizer, E.
A novel phosphopantetheine:protein transferase activating yeast mitochondrial acyl carrier protein
J. Biol. Chem.
273
22334-22339
1998
Saccharomyces cerevisiae (Q12036), Saccharomyces cerevisiae
brenda
Chirgadze, N.Y.; Briggs, S.L.; McAllister, K.A.; Fischl, A.S.; Zhao, G.
Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis
EMBO J.
19
5281-5287
2000
Streptomyces pneumoniae
brenda
Flugel, R.S.; Hwangbo, Y.; Lambalot, R.H.; Cronan, J.E., Jr.; Walsh, C.T.
Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
J. Biol. Chem.
275
959-968
2000
Escherichia coli, no activity in Escherichia coli, no activity in Escherichia coli MP4
brenda
McAllister, K.A.; Peery, R.B.; Meier, T.I.; Fischl, A.S.; Zhao, G.
Biochemical and molecular analyses of the Streptococcus pneumoniae acyl carrier protein synthase, an enzyme essential for fatty acid biosynthesis
J. Biol. Chem.
275
30864-30872
2000
Streptomyces pneumoniae, Streptomyces pneumoniae (P0A2W7)
brenda
Parris, K.D.; Lin, L.; Tam, A.; Mathew, R.; Hixon, J.; Stahl, M.; Fritz, C.C.; Seehra, J.; Somers, W.S.
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
Structure Fold. Des.
8
883-895
2000
Bacillus subtilis
brenda
Flaman, A.S.; Chen, J.M.; Van Iderstine, S.C.; Byers, D.M.
Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity
J. Biol. Chem.
276
35934-35939
2001
Vibrio harveyi (P0A2W3)
brenda
Gaitatzis, N.; Hans, A.; Mueller, R.; Beyer, S.
The mtaA gene of the myxothiazol biosynthetic gene cluster from Stigmatella aurantiaca DW4/3-1 encodes a phosphopantetheinyl transferase that activates polyketide synthases and polypeptide synthetases
J. Biochem.
129
119-124
2001
Stigmatella aurantiaca (Q9RFL1)
brenda
Sanchez, C.; Du, L.; Edwards, D.J.; Toney, M.D.; Shen, B.
Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-polyketide antitumor drug bleomycin
Chem. Biol.
8
725-738
2001
Streptomyces verticillus (Q9F0Q6), Streptomyces verticillus, Streptomyces verticillus ATCC 15003 (Q9F0Q6)
brenda
Chopra, S.; Singh, S.K.; Sati, S.P.; Ranganathan, A.; Sharma, A.
Expression, purification, crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (acpS) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
58
179-181
2002
Mycobacterium tuberculosis
brenda
Mofid, M.R.; Finking, R.; Marahiel, M.A.
Recognition of hybrid peptidyl carrier proteins/acyl carrier proteins in nonribosomal peptide synthetase modules by the 4'-phosphopantetheinyl transferases AcpS and Sfp
J. Biol. Chem.
277
17023-17031
2002
Bacillus subtilis
brenda
Mootz, H.D.; Schoergendorfer, K.; Marahiel, M.A.
Functional characterization of 4'-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5
FEMS Microbiol. Lett.
213
51-57
2002
Aspergillus nidulans, Brevibacillus brevis, Bacillus subtilis, Saccharomyces cerevisiae, no activity in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843, Aspergillus nidulans FGSC4
brenda
Joshi, A.K.; Zhang, L.; Rangan, V.S.; Smith, S.
Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity
J. Biol. Chem.
278
33142-33149
2003
Homo sapiens
brenda
Reed, M.A.C.; Schweizer, M.; Szafranska, A.E.; Arthur, C.; Nicholson, T.P.; Cox, R.J.; Crosby, J.; Crump, M.P.; Simpson, T.J.
The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs
Org. Biomol. Chem.
1
463-471
2003
Rattus norvegicus
brenda
Daubaras, D.L.; Wilson, E.M.; Black, T.; Strickland, C.; Beyer, B.M.; Orth, P.
Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus
Acta Crystallogr. Sect. D
60
773-774
2004
Staphylococcus aureus
brenda
Finking, R.; Mofid, M.R.; Marahiel, M.A.
Mutational analysis of peptidyl carrier protein and acyl carrier protein synthase unveils residues involved in protein-protein recognition
Biochemistry
43
8946-8956
2004
Bacillus subtilis
brenda
Gilbert, A.M.; Kirisits, M.; Toy, P.; Nunn, D.S.; Failli, A.; Dushin, E.G.; Novikova, E.; Petersen, P.J.; Joseph-McCarthy, D.; McFadyen, I.; Fritz, C.C.
Anthranilate 4H-oxazol-5-ones: novel small molecule antibacterial acyl carrier protein synthase (AcpS) inhibitors
Bioorg. Med. Chem. Lett.
14
37-41
2004
Bacillus subtilis
brenda
Weissman, K.J.; Hong, H.; Oliynyk, M.; Siskos, A.P.; Leadlay, P.F.
Identification of a phosphopantetheinyl transferase for erythromycin biosynthesis in Saccharopolyspora erythraea
ChemBioChem
5
116-125
2004
Saccharopolyspora erythraea
brenda
Cai, X.; Herschap, D.; Zhu, G.
Functional characterization of an evolutionarily distinct phosphopantetheinyl transferase in the apicomplexan Cryptosporidium parvum
Eukaryot. Cell
4
1211-1220
2005
Cryptosporidium parvum (Q5I4D4), Cryptosporidium parvum
brenda
Finking, R.; Solsbacher, J.; Konz, D.; Schobert, M.; Schfer, A.; Jahn, D.; Marahiel, M.A.
Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore synthesis in Pseudomonas aeruginosa
J. Biol. Chem.
277
50293-50302
2002
Pseudomonas aeruginosa
brenda
Barekzi, N.; Joshi, S.; Irwin, S.; Ontl, T.; Schweizer, H.P.
Genetic characterization of pcpS, encoding the multifunctional phosphopantetheinyl transferase of Pseudomonas aeruginosa
Microbiology
150
795-803
2004
Pseudomonas aeruginosa
brenda
Zhou, Z.; Cironi, P.; Lin, A.J.; Xu, Y.; Hrvatin, S.; Golan, D.E.; Silver, P.A.; Walsh, C.T.; Yin, J.
Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases
ACS Chem. Biol.
2
337-346
2007
Bacillus subtilis, Escherichia coli
brenda
Orikasa, Y.; Nishida, T.; Hase, A.; Watanabe, K.; Morita, N.; Okuyama, H.
A phosphopantetheinyl transferase gene essential for biosynthesis of n-3 polyunsaturated fatty acids from Moritella marina strain MP-1
FEBS Lett.
580
4423-4429
2006
Moritella marina, Moritella marina MP-1
brenda
McAllister, K.A.; Peery, R.B.; Zhao, G.
Acyl carrier protein synthases from Gram-negative, Gram-positive, and atypical bacterial species: Biochemical and structural properties and physiological implications
J. Bacteriol.
188
4737-4748
2006
Streptococcus pneumoniae, Mycoplasma pneumoniae, Escherichia coli (P24224)
brenda
Huang, Y.; Wendt-Pienkowski, E.; Shen, B.
A dedicated phosphopantetheinyl transferase for the fredericamycin polyketide synthase from Streptomyces griseus
J. Biol. Chem.
281
29660-29668
2006
Streptomyces griseus (Q2MGB1), Streptomyces griseus
brenda
Gong, H.; Murphy, A.; McMaster, C.R.; Byers, D.M.
Neutralization of acidic residues in helix II stabilizes the folded conformation of acyl carrier protein and variably alters its function with different enzymes
J. Biol. Chem.
282
4494-4503
2007
Vibrio harveyi
brenda
De Lay, N.R.; Cronan, J.E.
A genome rearrangement has orphaned the Escherichia coli K-12 AcpT phosphopantetheinyl transferase from its cognate Escherichia coli O157:H7 substrates
Mol. Microbiol.
61
232-242
2006
Escherichia coli
brenda
Bunkoczi, G.; Pasta, S.; Joshi, A.; Wu, X.; Kavanagh, K.L.; Smith, S.; Oppermann, U.
Mechanism and substrate recognition of human holo ACP synthase
Chem. Biol.
14
1243-1253
2007
Homo sapiens (Q9NRN7), Homo sapiens
brenda
Strickland, K.C.; Hoeferlin, L.A.; Oleinik, N.V.; Krupenko, N.I.; Krupenko, S.A.
Acyl carrier protein-specific 4-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase
J. Biol. Chem.
285
1627-1633
2010
Homo sapiens
brenda
Jiang, H.; Wang, Y.Y.; Ran, X.X.; Fan, W.M.; Jiang, X.H.; Guan, W.J.; Li, Y.Q.
Improvement of natamycin production by engineering of phosphopantetheinyl transferases in Streptomyces chattanoogensis L10
Appl. Environ. Microbiol.
79
3346-3354
2013
Streptomyces chattanoogensis (H9N836), Streptomyces chattanoogensis (H9N839), Streptomyces chattanoogensis, Streptomyces chattanoogensis L10 (H9N836), Streptomyces chattanoogensis L10 (H9N839), Streptomyces chattanoogensis L10
brenda
Owen, J.G.; Copp, J.N.; Ackerley, D.F.
Rapid and flexible biochemical assays for evaluating 4-phosphopantetheinyl transferase activity
Biochem. J.
436
709-717
2011
Bacillus subtilis, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas putida KT 2240, Bacillus subtilis ATCC 6633
brenda
Dallaglio, P.; Arthur, C.J.; Williams, C.; Vasilakis, K.; Maple, H.J.; Crosby, J.; Crump, M.P.; Hadfield, A.T.
Analysis of Streptomyces coelicolor phosphopantetheinyl transferase, AcpS, reveals the basis for relaxed substrate specificity
Biochemistry
50
5704-5717
2011
Streptomyces coelicolor
brenda
Owen, J.G.; Robins, K.J.; Parachin, N.S.; Ackerley, D.F.
A functional screen for recovery of 4'-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries
Environ. Microbiol.
14
1198-1209
2012
Escherichia coli
brenda
Allen, G.; Bromley, M.; Kaye, S.J.; Keszenman-Pereyra, D.; Zucchi, T.D.; Price, J.; Birch, M.; Oliver, J.D.; Turner, G.
Functional analysis of a mitochondrial phosphopantetheinyl transferase (PPTase) gene pptB in Aspergillus fumigatus
Fungal Genet. Biol.
48
456-464
2011
Aspergillus fumigatus, Aspergillus fumigatus Af293
brenda
Velazquez-Robledo, R.; Contreras-Cornejo, H.A.; Macias-Rodriguez, L.; Hernandez-Morales, A.; Aguirre, J.; Casas-Flores, S.; Lopez-Bucio, J.; Herrera-Estrella, A.
Role of the 4-phosphopantetheinyl transferase of Trichoderma virens in secondary metabolism and induction of plant defense responses
Mol. Plant Microbe Interact.
24
1459-1471
2011
Trichoderma virens
brenda
Leng, Y.; Zhong, S.
Sfp-type 4'-phosphopantetheinyl transferase is required for lysine synthesis, tolerance to oxidative stress and virulence in the plant pathogenic fungus Cochliobolus sativus
Mol. Plant Pathol.
13
375-387
2012
Bipolaris sorokiniana (G8DNT2), Bipolaris sorokiniana
brenda
Nair, D.R.; Ghosh, R.; Manocha, A.; Mohanty, D.; Saran, S.; Gokhale, R.S.
Two functionally distinctive phosphopantetheinyl transferases from amoeba Dictyostelium discoideum
PLoS ONE
6
e24262
2011
Dictyostelium discoideum (Q54MI2), Dictyostelium discoideum (Q552R4), Dictyostelium discoideum AX2 (Q54MI2), Dictyostelium discoideum AX2 (Q552R4)
brenda
Wiemann, P.; Albermann, S.; Niehaus, E.M.; Studt, L.; von Bargen, K.W.; Brock, N.L.; Humpf, H.U.; Dickschat, J.S.; Tudzynski, B.
The Sfp-type 4-phosphopantetheinyl transferase Ppt1 of Fusarium fujikuroi controls development, secondary metabolism and pathogenicity
PLoS ONE
7
e37519
2012
Fusarium fujikuroi, Fusarium fujikuroi IMI58289
brenda
Leblanc, C.; Prudhomme, T.; Tabouret, G.; Ray, A.; Burbaud, S.; Cabantous, S.; Mourey, L.; Guilhot, C.; Chalut, C.
4-Phosphopantetheinyl transferase PptT, a new drug target required for Mycobacterium tuberculosis growth and persistence in vivo
PLoS Pathog.
8
e1003097
2012
Mycobacterium tuberculosis, Mycobacterium tuberculosis BCG
brenda
Vickery, C.R.; Kosa, N.M.; Casavant, E.P.; Duan, S.; Noel, J.P.; Burkart, M.D.
Structure, biochemistry, and inhibition of essential 4'-phosphopantetheinyl transferases from two species of Mycobacteria
ACS Chem. Biol.
9
1939-1944
2014
Mycobacterium ulcerans (A0PU93), Mycobacterium tuberculosis (P9WQD3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQD3)
brenda
Wang, Y.Y.; Luo, H.D.; Zhang, X.S.; Lin, T.; Jiang, H.; Li, Y.Q.
The substrate promiscuity of a phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins
Arch. Microbiol.
198
193-197
2016
Streptomyces chattanoogensis (H9N839), Streptomyces chattanoogensis L10 (H9N839), Streptomyces chattanoogensis L10
brenda
Kumar, A.; Arya, R.; Makwana, P.K.; Dangi, R.S.; Yadav, U.; Surolia, A.; Kundu, S.; Sundd, M.
The structure of the holo-acyl carrier protein of Leishmania major displays a remarkably different phosphopantetheinyl transferase binding interface
Biochemistry
54
5632-5645
2015
Bacillus subtilis (P39135), Leishmania major (Q4QCW3), Leishmania major, Bacillus subtilis 168 (P39135)
brenda
Kosa, N.M.; Foley, T.L.; Burkart, M.D.
Fluorescent techniques for discovery and characterization of phosphopantetheinyl transferase inhibitors
J. Antibiot.
67
113-120
2014
Homo sapiens (Q9NRN7), Homo sapiens
brenda
Viala, J.P.; Puppo, R.; My, L.; Bouveret, E.
Posttranslational maturation of the invasion acyl carrier protein of Salmonella enterica serovar Typhimurium requires an essential phosphopantetheinyl transferase of the fatty acid biosynthesis pathway
J. Bacteriol.
195
4399-4405
2013
Salmonella enterica subsp. enterica serovar Typhimurium (P63466), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kim, J.M.; Song, H.Y.; Choi, H.J.; So, K.K.; Kim, D.H.; Chae, K.S.; Han, D.M.; Jahng, K.Y.
Characterization of NpgA, a 4'-phosphopantetheinyl transferase of Aspergillus nidulans, and evidence of its involvement in fungal growth and formation of conidia and cleistothecia for development
J. Microbiol.
53
21-31
2015
Aspergillus nidulans (Q9UVK7), Aspergillus nidulans, Aspergillus nidulans SNT611 (Q9UVK7)
brenda
Rottier, K.; Faille, A.; Prudhomme, T.; Leblanc, C.; Chalut, C.; Cabantous, S.; Guilhot, C.; Mourey, L.; Pedelacq, J.D.
Detection of soluble co-factor dependent protein expression in vivo: application to the 4'-phosphopantetheinyl transferase PptT from Mycobacterium tuberculosis
J. Struct. Biol.
183
320-328
2013
Mycobacterium tuberculosis (O33336), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (O33336)
brenda
Jung, J.; Bashiri, G.; Johnston, J.M.; Brown, A.S.; Ackerley, D.F.; Baker, E.N.
Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein
J. Struct. Biol.
188
274-278
2014
Mycobacterium tuberculosis (O33336), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (O33336)
brenda
Beld, J.; Sonnenschein, E.C.; Vickery, C.R.; Noel, J.P.; Burkart, M.D.
The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life
Nat. Prod. Rep.
31
61-108
2014
Bacillus anthracis, Brevibacillus brevis, Bacillus licheniformis, Streptomyces coelicolor, Streptomyces coelicolor (O86785), Streptomyces coelicolor (O88029), Xanthomonas albilineans (D2U8G6), Escherichia coli (E2QFX9), Escherichia coli (P19925), Escherichia coli (P24224), Escherichia coli (Q0P7J0), Bacillus subtilis (P39135), Mycobacterium tuberculosis (P9WQD3), Burkholderia cenocepacia (Q27IP6), Vibrio anguillarum (Q5DK20), Burkholderia pseudomallei (Q63I03), Yersinia pestis (Q74V64), Serratia marcescens (Q75PZ2), Pseudomonas aeruginosa (Q9I4H2), Vibrio cholerae (Q9RCF2), Bacillus subtilis 168 (P39135), Xanthomonas albilineans GPE PC73 (D2U8G6), Serratia marcescens Db11 (Q75PZ2), Vibrio anguillarum ATCC 68554 (Q5DK20), Pseudomonas aeruginosa DSM 22644 (Q9I4H2), Streptomyces coelicolor ATCC BAA-471 (O86785), Mycobacterium tuberculosis H37Rv (P9WQD3), Burkholderia pseudomallei K96243 (Q63I03)
brenda
Guan, X.; Chen, H.; Abramson, A.; Man, H.; Wu, J.; Yu, O.; Nikolau, B.J.
A phosphopantetheinyl transferase that is essential for mitochondrial fatty acid biosynthesis
Plant J.
84
718-732
2015
Arabidopsis thaliana (F4IRA7), Arabidopsis thaliana (Q8VYK1)
brenda
Contreras-Cornejo, H.; Macias-Rodriguez, L.; Herrera-Estrella, A.; Lopez-Bucio, J.
The 4-phosphopantetheinyl transferase of Trichoderma virens plays a role in plant protection against Botrytis cinerea through volatile organic compound emission
Plant Soil
379
261-274
2014
Trichoderma virens (G9MYY8), Trichoderma virens (G9N7J4)
-
brenda
Dobb, K.S.; Kaye, S.J.; Beckmann, N.; Thain, J.L.; Stateva, L.; Birch, M.; Oliver, J.D.
Characterisation of the Candida albicans phosphopantetheinyl transferase Ppt2 as a potential antifungal drug target
PLoS ONE
10
e0143770
2015
Candida albicans (Q5APF3), Candida albicans
brenda
Wang, Y.Y.; Zhang, X.S.; Luo, H.D.; Ren, N.N.; Jiang, X.H.; Jiang, H.; Li, Y.Q.
Characterization of discrete phosphopantetheinyl transferases in Streptomyces tsukubaensis L19 unveils a complicate phosphopantetheinylation network
Sci. Rep.
6
24255
2016
Streptomyces tsukubensis (A0A0X8EK72), Streptomyces tsukubensis (A0A0Y0S258), Streptomyces tsukubensis (A0A0Y0SAB4), Streptomyces tsukubensis (A0A109R3N8), Streptomyces tsukubensis (I2N4F3), Streptomyces tsukubensis, Streptomyces tsukubensis L19 (A0A0X8EK72), Streptomyces tsukubensis L19 (A0A0Y0S258), Streptomyces tsukubensis L19 (A0A0Y0SAB4), Streptomyces tsukubensis L19 (A0A109R3N8), Streptomyces tsukubensis L19 (I2N4F3)
brenda
Ma, J.C.; Wu, Y.Q.; Cao, D.; Zhang, W.B.; Wang, H.H.
Only acyl carrier protein 1 (AcpP1) functions in Pseudomonas aeruginosa fatty acid synthesis
Front. Microbiol.
8
2186
2017
Pseudomonas aeruginosa (Q9I4H2)
brenda
Hitschler, J.; Boles, E.
De novo production of aromatic m-cresol in Saccharomyces cerevisiae mediated by heterologous polyketide synthases combined with a 6-methylsalicylic acid decarboxylase
Metab. Eng. Commun.
9
e00093
2019
Aspergillus nidulans (G5EB87), Aspergillus nidulans
brenda
Lauciello, L.; Lack, G.; Scapozza, L.; Perozzo, R.
A high yield optimized method for the production of acylated ACPs enabling the analysis of enzymes involved in P. falciparum fatty acid biosynthesis
Biochem. Biophys. Rep.
8
310-317
2016
Escherichia coli (P24224)
brenda
Biswas, R.; Singh, B.K.; Dutta, D.; Das, P.K.; Maiti, M.K.; Basak, A.; Das, A.K.
Decrypting the oscillating nature of the 4-phosphopantetheine arm in acyl carrier protein AcpM of Mycobacterium tuberculosis
FEBS Lett.
593
622-633
2019
Bacillus subtilis (P39135), Bacillus subtilis 168 (P39135)
brenda
Sonnenschein, E.; Pu, Y.; Beld, J.; Burkart, M.
Phosphopantetheinylation in the green microalgae Chlamydomonas reinhardtii
J. Appl. Phycol.
28
3259-3267
2016
Chlamydomonas reinhardtii (A8HPQ6), Chlamydomonas reinhardtii (A8I7F7)
-
brenda
Marcella, A.M.; Culbertson, S.J.; Shogren-Knaak, M.A.; Barb, A.W.
Structure, high affinity, and negative cooperativity of the Escherichia coli holo-(acyl carrier protein) holo-(acyl carrier protein) synthase complex
J. Mol. Biol.
429
3763-3775
2017
Escherichia coli (P24224)
brenda
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