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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]
? + holo-[acyl-carrier protein]
acetoacetyl-CoA + apo-[acyl-carrier protein]
CoA + acetoacetyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
apo-[acyl-carrier protein] + acetyl-CoA
CoA + acetyl-[acyl-carrier protein]
pH 7, 37°C
reaction stop by 10% trichloroacetic acid, limited release of 3â,5â-ADP by interactions with guanidinium moieties of R74 and R86
-
?
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
-
-
-
-
r
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
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 + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
butanoyl-CoA + apo-[acyl-carrier protein]
CoA + butanoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[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]
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-[EntB-ArCP-H6 E. coli]
? + holo-[acyl-carrier protein]
-
-
-
-
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-[PCPH6SrfB1.18]
? + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[PCPH6SrfB2.18]
? + 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-peptide(1->74)
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
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-[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]
? + holo-[acyl-carrier protein]
crotonyl-CoA + apo-[acyl-carrier protein]
CoA + crotonyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[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]
-
-
?
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[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]
? + holo-[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]
? + holo-[acyl-carrier protein]
myristoyl-CoA + apo-[acyl-carrier protein]
CoA + myristoyl-[acyl-carrier protein]
substrate Plasmodium falciparum apo-[acyl-carrier protein]
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[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
additional information
?
-
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]
-
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]
-
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]
-
-
-
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-peptide(1->74)

?
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-peptide(1->74)
?
-
-
-
-
?
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
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?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
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-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]

adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
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?
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)
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?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
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-
-
?
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
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-
?
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
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-
?
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
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?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
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-
?
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
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-
?
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
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-
?
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
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-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
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-
?
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
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-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
broad specificity of the single PPTase
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-
?
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]
-
-
-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
?
-
-
3'-dephospho-CoA is no substrate
-
-
?
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 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 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
?
-
-
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
?
-
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.
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]
additional information
?
-
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]
-
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]
-
-
-
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]
-
-
-
?
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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