Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.8.7
-
RECOMMENDED NAME
GeneOntology No.
holo-[acyl-carrier-protein] synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acyl carrier protein activation
-
-
acyl carrier protein metabolism
-
-
enterobactin biosynthesis
-
-
lipid metabolism
-
-
Pantothenate and CoA biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
CoA-[4'-phosphopantetheine]:apo-[acyl-carrier protein] 4'-pantetheinephosphotransferase
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-30-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
strain FGSC4
-
-
Manually annotated by BRENDA team
strain FGSC4
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolate ND90Pr (ATCC 201652)
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain MP-1
-
-
Manually annotated by BRENDA team
strain MP-1
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
strain MP4, denoted acpS1 gene
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli MP4
strain MP4, denoted acpS1 gene
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
yeast, strain lys5
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
castor-oil-seed, L. cv. Baker 296
-
-
Manually annotated by BRENDA team
strain ATCC24843
-
-
Manually annotated by BRENDA team
strain ATCC24843
-
-
Manually annotated by BRENDA team
Melody
-
-
Manually annotated by BRENDA team
strain DW4/3-1, gene mtaA
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Streptomyces pneumoniae
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
Manually annotated by BRENDA team
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
show the reaction diagram
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
show the reaction diagram
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
show the reaction diagram
apo-[acyl-carrier protein] + acetyl-CoA
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
pH 7, 37C
reaction stop by 10% trichloroacetic acid, limited release of 3,5-ADP by interactions with guanidinium moieties of R74 and R86
-
?
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
show the reaction diagram
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
show the reaction diagram
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
show the reaction diagram
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
show the reaction diagram
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
show the reaction diagram
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
show the reaction diagram
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
show the reaction diagram
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
show the reaction diagram
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
show the reaction diagram
-
-
-
-
r
CoA + apo-[EntB-ArCP-H6 E. coli]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[fredericamycin H acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[fredericamycin acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA + apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[PCPH6SrfB1.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[PCPH6SrfB2.18]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
CoA + apo-[peptidyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
show the reaction diagram
-
-
-
-
?
CoA + apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. frenolicin-acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[Streptomyces sp. granaticin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. granaticin-acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
CoA + apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
show the reaction diagram
-
-
-
-
r
CoA + apo-[tetracenomycin M acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[tetracenomycin M acyl-carrier protein]
show the reaction diagram
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
show the reaction diagram
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
show the reaction diagram
CoA-[4'-phosphopantetheine] + apo-[FDH protein]
adenosine 3',5'-bisphosphate + holo-[FDH protein]
show the reaction diagram
-
the enzyme modifies the apo-FDH protein at serine 354 and activates its catalysis
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
desulfoCoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
? + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
myristoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
palmitoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
phenylacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
show the reaction diagram
-
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]
show the reaction diagram
-
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phosphopantetheine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
-
IC50: 0.0021 mM
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.015 mM
3',5'-ADP
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0015 mM
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0034 mM
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.002 mM
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00013 mM
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0011 mM
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0019 mM
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0013 mM
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00027 mM
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.0044 mM
-
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
-
IC50: 0.00083 mM
-
6-nitroso-1,2-benzopyrone
apo-acyl-carrier protein
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apo-acyl-carrier protein
Streptomyces pneumoniae
significantly stimulating above 0.01 mM
CoA
-
stimulates the holoACP synthase reaction within the intact organelle
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0088 - 0.051
acetoacetyl-CoA
0.0077 - 0.399
acetyl-CoA
0.017 - 0.068
apo-ACP
0.0002 - 0.072
apo-acyl-carrier protein
0.002
apo-peptide(1-->74)
0.00445 - 0.026
apo-peptidyl carrier protein
0.0008 - 0.0018
apo-[acyl-carrier protein]
0.0033 - 0.0086
apo-[BpsA protein]
0.016
apo-[EntB-ArCP-H6 Escherichia coli]
-
pH 6.0, 37C
-
0.0058
apo-[fredericamycin H acyl-carrier protein]
pH 8.0, 37C
0.005
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
-
pH 6.0, 37C
-
0.0018
apo-[PCPH6SrfB2.18]
-
pH 6.0, 37C
-
0.0031 - 0.0039
apo-[peptidyl carrier protein]
0.012
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.005
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.039
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.022
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
pH 7.0, 37C, Escherichia coli acyl carrier protein
0.1
apo-[tetracenomycin M acyl-carrier protein]
pH 8.0, 37C
0.007 - 0.035
Butyryl-CoA
0.0011 - 0.15
CoA
0.00062 - 0.011
CoA-[4'-phosphopantetheine]
0.0052 - 0.018
crotonyl-CoA
0.0014 - 0.0015
decanoyl-CoA
0.123 - 0.242
DSLEFIASKLA
0.117 - 0.534
GDSLDMLEWSLM
0.108 - 0.12
GDSLSWLLRCLN
0.0515 - 0.076
GDSLSWLLRLLN
0.221 - 0.254
GDSLSWLLRSLN
0.0772 - 0.139
GDSLSWLVRCLN
0.0618 - 0.105
GDSLSWLVRLLN
0.0071 - 0.094
malonyl-CoA
0.44 - 104.1
Mg2+
0.0025
myristoleoyl-CoA
-
pH 7.5, 22C
0.001 - 0.0018
myristoyl-CoA
0.0009 - 0.0016
palmitoleoyl-CoA
0.0012
palmitoyl-CoA
-
pH 7.5, 22C
additional information
acetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.2
acetoacetyl-CoA
0.000098 - 0.973
acetyl-CoA
0.0283 - 2.08
apo-acyl-carrier protein
0.239 - 1.6
apo-peptidyl carrier protein
0.002 - 0.7
apo-[acyl-carrier protein]
0.035 - 0.683
apo-[BpsA protein]
1.08
apo-[EntB-ArCP-H6 Escherichia coli]
Bacillus subtilis
-
pH 6.0, 37C
-
0.75 - 0.95
apo-[fredericamycin H acyl-carrier protein]
1.17
apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
Bacillus subtilis
-
pH 6.0, 37C
-
1.73
apo-[PCPH6SrfB1.18]
Bacillus subtilis
-
pH 6.0, 37C
-
0.933
apo-[PCPH6SrfB2.18]
Bacillus subtilis
-
pH 6.0, 37C
-
0.183 - 1.43
apo-[peptidyl carrier protein]
0.317
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.5
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.167
apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.09
apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
Escherichia coli
-
pH 7.0, 37C, E. coli ACP
0.004 - 0.3
Butyryl-CoA
0.002 - 2.8
CoA
0.0027 - 0.075
CoA-[4'-phosphopantetheine]
0.005 - 0.2
crotonyl-CoA
0.004 - 0.5
decanoyl-CoA
0.013 - 0.18
DSLEFIASKLA
0.004 - 0.03
GDSLDMLEWSLM
0.001 - 0.17
GDSLSWLLRCLN
0.0005 - 0.17
GDSLSWLLRLLN
0.0013 - 0.14
GDSLSWLLRSLN
0.0007 - 0.07
GDSLSWLVRCLN
0.0005 - 0.05
GDSLSWLVRLLN
0.0004 - 0.1
malonyl-CoA
0.0003 - 1.2
Mg2+
0.5
myristoleoyl-CoA
Streptococcus pneumoniae
-
pH 7.5, 22C
0.003 - 0.5
myristoyl-CoA
0.4
palmitoleoyl-CoA
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.7 - 108
apo-[BpsA protein]
3.3 - 20
CoA-[4'-phosphopantetheine]
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
3',5'-ADP
Streptomyces pneumoniae
pH 7.0, 37C
0.00042 - 0.0052
6-nitroso-1,2-benzopyrone
0.002
apo-acyl-carrier protein
-
pH 7.0, 37C, E. coli ACP
0.054
apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
pH 7.0, 37C, E. coli ACP
0.0006
apo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
pH 7.0, 37C, E. coli ACP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-5-fluoro-benzoic acid
Bacillus subtilis
-
IC50: 0.0021 mM
0.015
2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.015 mM
0.0015
5-bromo-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0015 mM
0.0034
5-bromo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0034 mM
0.002
5-bromo-4-chloro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.002 mM
0.00013
5-carboxyamino-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00013 mM
0.0011
5-chloro-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0011 mM
0.0019
5-fluoro-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0019 mM
0.0013
5-iodo-2-[[2-(4-chloro-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0013 mM
0.00027
5-methyl-2-[[2-(3-fluoro-4-trifluoromethyl-phenyl)-5-oxo-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00027 mM
0.0044
5-methyl-2-[[5-oxo-2-(3-trifluoromethoxy-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.0044 mM
-
0.00083
5-methyl-2-[[5-oxo-2-(4-trifluoromethyl-phenyl)-oxazolidin-(4E)-ylidenemethyl]-amino]-benzoic acid
Bacillus subtilis
-
IC50: 0.00083 mM
-
0.0021 - 0.0108
6-nitroso-1,2-benzopyrone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0012
-
wild-type
additional information
-
specific activity 88.0 units/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
-
less than 20% of maximum activity at both pH 5.0 and 7.0, 50% of activity maximum at pH 5.5 and pH 6.8
5 - 7
-
pH 5: less than 27% of maximal activity, pH 7: less than 62% of maximal activity, activity with apo-[acyl-carrier protein]
6 - 11
-
about 20% of activity maximum at pH 6.5, about 30% of activity maximum at pH 11.0
7 - 8.8
-
half maximal activity at pH 7.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
Streptomyces pneumoniae
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.25
-
calculated from molar extinction coefficient by the method of Gill and von Hippel
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium ulcerans (strain Agy99)
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13390
Streptomyces pneumoniae
AcpS, calculated from predicted amino acid sequence; AcpS, mass spectrometric analysis
20320
mitochondrial isoenzyme, calculated from open reading frame
21000
mitochondrial isoenzyme, SDS-PAGE
26830
calculated from amino acid sequence of His6-tagged svp
27000
-
C-terminal His6-tag fusion protein, gel filtration
31600
gel filtration
38000
Streptomyces pneumoniae
purified AcpS, gel filtration
39000
Streptomyces pneumoniae
AcpS, sedimentation analysis
41000
Streptomyces pneumoniae
AcpS, native homotrimer, predicted from nucleotide sequence
50000
-
gel filtration, sucrose density gradient sedimentation
53000
Streptomyces pneumoniae
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-crystallized with CoA and ACP
-
apo-PPT (PDB: 2BYD) or in complex with coenzyme A (CoA, 5 mM) and Mg2+ (20 mM) (PDB: 2C43) or coenzyme A (2.5 mM) and acyl-carrier protein (S2156A mutant of ACP domain of fatty acid synthase) (PDB: 2CG5), precipitant: 14% PEG3350 and 0.05 M H3Cit/Na3Cit pH 5.7 or 2 M NaCl and 10% PEG6000 (complexes), apo-PPT: space group: P2(1)2(1)2(1), unit cell parameters: a: 63.78, b: 69.95, c: 71.24, alpha/beta fold with pseudo 2fold symmetry, N-terminal beta sheet (residues 91-116) connected to C-terminal beta sheet (residues 207-239) by a one residue linker and unique N-terminal and C-terminal extensions of 13 and 52 amino acids, respectively, PPT-CoA complex: space group: P2(1)2(1)2(1), unit cell parameters: a: 65.59, b: 68.96, c: 70.75, CoA-binding at the interface of N- and C-terminal domain mediated by PPT residues 47, 86, 110, 111, 185 (hydrophobic interactions, hydrogen bonds and salt bridges), and independent of Mg2+, Mg2+ bound through PPT residues 181 and 129 and coordinated by a water molecule, PPT-CoA-ACP complex: space group: P3(2)21, unit cell parameters: a, b: 69.36, c: 184.7, ACP-binding in the cleft between N- and C-terminal domain causes their rotation and slight closure, and is facilitated predominantly by hydrophobic interactions with PPT residues 51-54, 191, 144-148, 173, and 177 and a few polar interactions, disorder of C-terminal coil (residues 290-305), lack of Mg2+
crystallized by vapour-diffusion method, crystals belong to space group R3, with unit cell parameters a = b = 68.53, c = 85.9 A
-
hanging-drop vapor-diffusion method
-
complexed with CoA and acetyl-CoA, and mutant enzymes H110A and D111A, vapor diffusion method. Crystals of the AcpS-CoA-Mg2+ complex are obtained at 18C, from 0.3 M potassium thiocyanate (KSCN), 0.1 M sodium cacodylate (NaCac) (pH 6.5), and 15% (w/v) PEG 4000. The best diffracting crystal of the AcpS-acetyl-CoA complex is obtained in 0.2 M lithium sulfate, 25% (w/v) PEG 2000 MME, and 0.1 M NaCac (pH 6.5), in the presence of 5 mM acetyl-CoA. The D111A mutant crystallizes in 0.2 M KSCN, 0.1 M NaCac (pH 6.5), 8% (w/v) PEG 20000, and 8% (w/v) PEG 550 MME. The H110A mutant crystal is obtained in 0.3 Ms odium acetate, 0.1 M NaCac (pH 6.5), and 25% (w/v) PEG 2000 MME
-
-
Streptomyces pneumoniae
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 65
Streptomyces pneumoniae
stable in this range
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite heat labile, unstable during chromatographic procedures intended for its purification, can only be partially overcome by Mg2+ and dithiothreitol, addition of ethylene glycol, glycerol, EDTA or proteinase inhibitors failed to stabilize the plant enzyme
-
stable when CoA is present at half-saturating concentrations
-
very unstable, markedly protected from inactivation by the presence of half-saturating concentrations of reduced CoA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196C, stored in liquid nitrogen, enzyme maintains full activity for at least 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AcpS mutant enzymes
-
amylose affinity column chromatography
-
from bacterial lysate by immobilized metal affinity chromatography followed by gel filtration chromatography on Superdex200 HiLoad 26/60 column and concentration to 20 mg/ml or anion exchange chromatography and dialysis
Ni-NTA agarose column chromatography; Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and Sephadex G-25 gel filtration
-
Ni-NTA column chromatography; Ni-NTA column chromatography
Ni2+ affinity column chromatography and Superdex 75 gel filtration
-
partially
purified as fatty acid synthetase complex
-
recombinant C-terminal His6-tag fusion protein
-
recombinant enzyme
recombinant enzyme, expressed in Escherichia coli
recombinant enzyme, expressed in Escherichia coli BL21(DE3)pACPS1
-
recombinant enzyme, expressed in Escherichia coli DH5alpha
-
recombinant enzyme, expressed in Escherichia coli MV1190/pUC8-Sfp
-
recombinant isoenzymes AcpS and Sfp, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; genes acpS and acpP cloned and overexpressed in Escherichia coli, acpS complements an Escherichia coli mutant
Streptomyces pneumoniae
acpP gene amplified from a genomic Vibrio harveyi library by PCR, cloned and transformed in to Escherichia coli Bl-21
acpP gene cloned, sequenced and expressed in Escherichia coli
-
cloned and expressed in Sf9 insect cells
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cloned in Escherichia coli DH5alpha and overexpressed in Escherichia coli MV1190/pUC8-Sfp
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CpSFP-PPT is expressed from an artificially synthesized gene with codon usage optimized for Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-codon plus cells
-
expressed in Escherichia coli BL21(DE3)DELTAentD cells
-
expression in Escherichia coli
expression in Escherichia coli, mutant enzymes
-
from genomic DNA in pET23 for expression with C-terminal hexa-His tag and binding studies with Vibrio fischeri holo-ACP
gene acpP cloned and overproduced from recombinant Escherichia coli BL21(DE3)pDPJ
-
gene acpS cloned and expressed in Escherichia coli BL21(DE3)
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in pCOEX1 for expression with TEV protease-cleavable N-terminal hexa-His-tag in Escherichia coli BL21(DE3)-R3
mtaA gene of myxothiazol biosyntheic gene cluster, heterlogous coexpression with an acyl carrier protein domain in Escherichia coli XL1blue
open reading frame YPL148C is the potential mitochondrial PPTase gene, expressed in Escherichia coli and Saccharomyces cerevisiae
overexpression as a C-terminal His6-tag fusion protein in Escherichia coli
-
PPT1 cloned and expressed in Escherichia coli DH5alpha
-
PPTase gene gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
PPtase gene npgA complements the lys5 deletion in Saccharomyces cerevisiae
-
PPtase gene q10474, the putative lys7 gene, complements the lys5 deletion in Saccharomyces cerevisiae
-
PPTase gene Sfp and Gsp complemented the lys5 deletion in Saccharomyces cerevisiae
-
recombinant ACP synthase overproduced in Escherichia coli BL21(DE3)pACPS1
-
region from the rat FAS including putative acyl carrier protein cloned and overexpressed in Escherichia coli strains DH5alpha and BL21(DE3)
-
sequenced
Streptomyces pneumoniae
-
sfp and acpS cloned and overproduced in Escherichia coli M15
-
svp gene cloned into pQE-70 and overproduced in Escherichia coli M15(pREP4)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D107E
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
E151A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G105D
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
G113Q
-
site-directed mutagenesis
I5R
-
site-directed mutagenesis
K155A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
K44A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
Q113R
-
site-directed mutagenesis
R14A
-
mutant enzyme exhibits catalytic efficiencies that are diminished by factor 500 compared to wild-type enzyme
W147A
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
W147F
-
site-directed mutagenesis of the sfp gene, constructed using the SOE method
D129A
reduced Mg2+ affinity and catalytic efficiency, D129 plays a role in Mg2+-coordination
E181A
significant loss in enzyme activity, reduced Mg2+ affinity and catalytic efficiency
E181Q
significant loss in enzyme activity, reduced Mg2+ affinity (20fold) and catalytic efficiency (300fold)
K185
significant loss in enzyme activity, reduced catalytic efficiency
Q112E
slightly reduced catalytic efficiency
Q112E, E181Q
double mutant, reduced Mg2+ affinity (200fold) and catalytic efficiency
R47A
reduced coenzymeA and Mg2+ affinity, increased catalytic efficiency
R86A
reduced coenzymeA and Mg2+ affinity, increased catalytic efficiency
D111A
-
active site mutant exhibiting 5% of wild type activity
E57A
-
active site mutant without any activity
H110A
-
active site mutant exhibiting 28% of wild type activity
R15A
-
active site mutant exhibiting 15% of wild type activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
enzyme can be utilized in an assay for apo-ACP in biological material
biotechnology
medicine
molecular biology
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