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Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase and Organism(s) Bacillus subtilis and UniProt Accession P39135

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EC Tree
IUBMB 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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Bacillus subtilis
UNIPROT: P39135
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, sfp-pptase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4'-phosphopantetheinyl transferase
-
phosphopantetheinyl transferase
-
surfactin phosphopantetheinyl transferase
-
4-phosphopantetheinyl transferase
-
-
acyl carrier protein holoprotein (holo-ACP) synthetase
-
-
-
-
acyl carrier protein synthase
-
-
acyl carrier protein synthetase
-
-
-
-
coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase
-
-
-
-
holo-ACP synthase
-
-
-
-
holo-ACP synthetase
-
-
-
-
holosynthase
-
-
-
-
phosphopantetheinyl transferase
-
-
surfactin synthetase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-30-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
show the reaction diagram
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]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
show the reaction diagram
-
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
show the reaction diagram
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[EntB-ArCP-H6 E. coli]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[PCPH6SrfB1.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[PCPH6SrfB2.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
show the reaction diagram
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[EntB-ArCP-H6 Escherichia coli]
?
show the reaction diagram
-
-
-
-
?
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
phenylacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phosphopantetheine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
complete inhibition at 50 mM
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
6-nitroso-1,2-benzopyrone
-
-
additional information
-
no substantial inhibition of Sfp by apo-[PCPH6SrfB1.18]
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038 - 0.215
apo-[acyl-carrier protein]
0.038 - 0.068
apo-ACP
0.0002 - 0.006
apo-acyl-carrier protein
0.00445 - 0.026
apo-peptidyl carrier protein
0.0033
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
-
0.016
apo-[EntB-ArCP-H6 Escherichia coli]
-
pH 6.0, 37°C
-
0.005
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
-
pH 6.0, 37°C
-
0.0018
apo-[PCPH6SrfB2.18]
-
pH 6.0, 37°C
-
0.007
CoA
-
pH 6.0, 37°C
0.00062
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
0.123
DSLEFIASKLA
-
-
0.534
GDSLDMLEWSLM
-
-
0.12
GDSLSWLLRCLN
-
-
0.0515
GDSLSWLLRLLN
-
-
0.221
GDSLSWLLRSLN
-
-
0.139
GDSLSWLVRCLN
-
-
0.0618
GDSLSWLVRLLN
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017 - 0.0192
apo-[acyl-carrier protein]
0.0283 - 2.08
apo-acyl-carrier protein
0.239 - 1.6
apo-peptidyl carrier protein
0.035
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
-
1.08
apo-[EntB-ArCP-H6 Escherichia coli]
-
pH 6.0, 37°C
-
1.17
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
-
pH 6.0, 37°C
-
1.73
apo-[PCPH6SrfB1.18]
-
pH 6.0, 37°C
-
0.933
apo-[PCPH6SrfB2.18]
-
pH 6.0, 37°C
-
0.0027
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
0.18
DSLEFIASKLA
-
-
0.004
GDSLDMLEWSLM
-
-
0.17
GDSLSWLLRCLN
-
-
0.17
GDSLSWLLRLLN
-
-
0.14
GDSLSWLLRSLN
-
-
0.07
GDSLSWLVRCLN
-
-
0.05
GDSLSWLVRLLN
-
-
additional information
additional information
-
turnover numbers with mutants of peptidyl-carrier protein as substrate
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
108
apo-[BpsA protein]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
-
3.5
CoA-[4'-phosphopantetheine]
-
in 100 mM Tris-HCl, pH 7.8, at 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00042 - 0.00053
6-nitroso-1,2-benzopyrone
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0021 - 0.0091
6-nitroso-1,2-benzopyrone
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 42–48 aa for AcpS (family I) and 38–41 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
monomer
-
isoenzyme AcpS
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-crystallized with CoA and ACP
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
G113Q
-
site-directed mutagenesis
I5R
-
site-directed mutagenesis
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
Q113R
-
site-directed mutagenesis
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Bacillus subtilis from Escherichia coli
AcpS mutant enzymes
-
Ni-NTA column chromatography
-
recombinant enzyme, expressed in Escherichia coli MV1190/pUC8-Sfp
-
recombinant isoenzymes AcpS and Sfp, expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BSU03570, recombinant expression of His-tagged enzyme from Bacillus subtilis in Escherichia coli
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
cloned in Escherichia coli DH5alpha and overexpressed in Escherichia coli MV1190/pUC8-Sfp
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli, mutant enzymes
-
PPTase gene Sfp and Gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
sfp and acpS cloned and overproduced in Escherichia coli M15
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
identification of short peptide tags of 12 residues as efficient substrate for site-specific protein labeling catalyzed by enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Aspergillus nidulans FGSC4, Bacillus subtilis, Brevibacillus brevis, no activity in Saccharomyces cerevisiae, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Bacillus subtilis ATCC 6633, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas putida KT 2240
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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, Bacillus licheniformis, Bacillus subtilis (P39135), Bacillus subtilis 168 (P39135), Brevibacillus brevis, Burkholderia cenocepacia (Q27IP6), Burkholderia pseudomallei (Q63I03), Burkholderia pseudomallei K96243 (Q63I03), Escherichia coli (E2QFX9), Escherichia coli (P19925), Escherichia coli (P24224), Escherichia coli (Q0P7J0), Mycobacterium tuberculosis (P9WQD3), Mycobacterium tuberculosis H37Rv (P9WQD3), Pseudomonas aeruginosa (Q9I4H2), Pseudomonas aeruginosa DSM 22644 (Q9I4H2), Serratia marcescens (Q75PZ2), Serratia marcescens Db11 (Q75PZ2), Streptomyces coelicolor, Streptomyces coelicolor (O86785), Streptomyces coelicolor (O88029), Streptomyces coelicolor ATCC BAA-471 (O86785), Vibrio anguillarum (Q5DK20), Vibrio anguillarum ATCC 68554 (Q5DK20), Vibrio cholerae (Q9RCF2), Xanthomonas albilineans (D2U8G6), Xanthomonas albilineans GPE PC73 (D2U8G6), Yersinia pestis (Q74V64)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team