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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase
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EC Tree
1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductaseIUBMB Comments
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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Word Map
- 1.1.1.100
-
enoyl
- drug development
- 3-oxoacyl-acps
-
transacylase
-
3-oxoacyl-acyl-carrier-protein
-
dehydrase
- fas-ii
- enoyl-acp
-
beta-hydroxyacyl-acp
- 4'-phosphopantetheine
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
3-ketoacyl acyl carrier protein reductase, 3-ketoacyl-(acyl-carrier-protein) reductase, 3-ketoacyl-ACP reductase, 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-ACP(CoA) reductase, 3-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-thioester reductase, 3-ketoacyl-[acyl-carrier-protein] reductase, 3-oxo-acyl-ACP reductase, 3-oxoacyl-(acyl carrier protein) reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl acyl carrier protein reductase
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-
-
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3-ketoacyl-acyl carrier protein reductase
3-ketoacyl-[acyl-carrier-protein] reductase
-
3-oxoacyl-ACP reductase
3-oxoacyl-AcpM reductase
3-oxoacyl-thioester reductase
3-oxoacyl-[ACP]reductase
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-
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beta-ketoacyl acyl carrier protein (ACP) reductase
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-
-
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beta-ketoacyl acyl carrier protein reductase
beta-ketoacyl reductase
beta-ketoacyl thioester reductase
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-
-
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beta-ketoacyl-ACP reductase
beta-ketoacyl-acyl carrier protein reductase
beta-ketoacyl-[acyl-carrier protein] (ACP) reductase
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-
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BKR
FabG
FabG1
fabG4
ketoacyl-acyl carrier protein reductase
MSMEG_6753
NADPH-dependent acetoacetyl coenzyme A reductase
NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
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-
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PHA-specific acetoacetyl-CoA reductase
PhaB
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
reductase, 3-oxoacyl-[acyl carrier protein]
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-
-
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3-ketoacyl-acyl carrier protein reductase
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-
-
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beta-ketoacyl reductase
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-
-
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beta-ketoacyl-ACP reductase
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-
-
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beta-ketoacyl-acyl carrier protein reductase
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-
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beta-ketoacyl-acyl carrier protein reductase
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ketoacyl-acyl carrier protein reductase
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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NADPH-dependent acetoacetyl coenzyme A reductase
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
belongs to family of short-chain alcohol dehydrogenases (SDR) with catalytic triad Ser154, Tyr167 and Lys171, catalytic mechanism
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a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
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-
-
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a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
ordered bi bi kinetic mechanism, [acyl-carrier protein] recognition mechanism
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
reaction mechanism, random bi bi kinetic mechanism
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a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
chemical and kinetic mechanism
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a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
cofactor and substrate binding kinetics, allosteric regulation mechanism, overview
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a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
positive cooperativity in binding of NADPH to enzyme, no cooperativity in binding of acetoacyl-CoA. Pre-existing equilibrium of two forms of free MabA in solution followed by a bimolecular association process
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
reduction
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redox reaction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(5Z)-dodecenoate biosynthesis I, (5Z)-dodecenoate biosynthesis II, 8-amino-7-oxononanoate biosynthesis I, cis-vaccenate biosynthesis, fatty acid elongation -- saturated, gondoate biosynthesis (anaerobic), mycolate biosynthesis, myristate biosynthesis (mitochondria), octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast), oleate biosynthesis IV (anaerobic), palmitate biosynthesis II (bacteria and plant cytoplasm), palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate), petroselinate biosynthesis, stearate biosynthesis II (bacteria and plants), superpathway of mycolate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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CAS REGISTRY NUMBER
COMMENTARY
37250-34-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
beta-oxidation pathway
-
-
?
1,1,1-trifluoroacetone + NADPH
? + NADP+
792% relative activity compared to acetophenone
-
-
?
2',3',4',5',6'-pentafluoroacetophenone + NADPH
? + NADP+
3023% relative activity compared to acetophenone
-
-
?
2-octanone + NADPH
? + NADP+
15% relative activity compared to acetophenone
-
-
?
3'-fluoroacetophenone + NADPH
? + NADP+
100% relative activity compared to acetophenone
-
-
?
3-hydroxydecanoyl-N-acetylcysteamine + NADP+
3-oxodecanoyl-N-acetylcysteamine + NADPH + H+
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
4'-chloroacetophenone + NADPH
? + NADP+
115% relative activity compared to acetophenone
-
-
?
4'-fluoroacetophenone + NADPH
? + NADP+
62% relative activity compared to acetophenone
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-
?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
acetoacetyl-CoA + NADPH
? + NADP+
-
wild-type shows less activity with acetoacetyl-CoA than with acetoacetyl-[acyl-carrier protein]
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-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
acetophenone + NADPH
? + NADP+
100% relative activity
-
-
?
alpha-chloroacetophenone + NADPH
? + NADP+
1885% relative activity compared to acetophenone
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
beta-ketobutyryl-CoA + NADPH
beta-hydroxybutyryl-CoA + NADP+
-
complementation of Escherichia coli fabG mutant with Lactobacillus lactis fabG genes shows that fabG1 encodes a functional beta-ketoacyl ACP reductase and fabG2 encodes an enzyme that has activity with the model substrate beta-ketobutyryl-CoA, but lacks the ability to support fatty acid synthesis both in vivo and in vitro
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-
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ethyl 4-chloroacetoacetate + NADPH
? + NADP+
29454% relative activity compared to acetophenone
-
-
?
ethylbenzoylacetate + NADPH
? + NADP+
892% relative activity compared to acetophenone
-
-
?
methyl acetoacetate + NADPH
? + NADP+
-
is not a good substrate as ethyl acetoacetate
-
-
?
propiophenone + NADPH
? + NADP+
123% relative activity compared to acetophenone
-
-
?
propyl acetoacetate + NADPH
? + NADP+
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as substrate it is limited to its weak solubility
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
belongs to family of short-chain alcohol dehydrogenases (SDR) with catalytic triade Ser154, Tyr167 and Lys171, catalytic mechanism
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme is part of the dissociable fatty acid synthase type II multienzyme complex for de novo synthesis of fatty acids from acetyl-CoA and malonyl-CoA
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
pH 6.0-7.0, equilibrium almost completely favors formation of the beta-hydroxyacyl ACP derivatives
product is the D-(-)-stereoisomer
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
-
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding
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-
r
3-oxododecanoyl-CoA + NADPH
(R)-3-hydroxydodecanoyl-CoA + NADP+
-
-
-
?
3-oxohexanoyl-CoA + NADH + H+
(3R)-3-hydroxyhexanoyl-CoA + NAD+
-
-
-
-
?
3-oxohexanoyl-CoA + NADH + H+
(3R)-3-hydroxyhexanoyl-CoA + NAD+
-
-
-
?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
-
-
-
-
?
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
?
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
-
-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
-
-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
much greater specificity for acetoacetyl-ACP than for either of the model substrates acetoacetyl-CoA or acetoacetyl-N-acetylcysteamine
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
much greater specificity for acetoacetyl-ACP than for either of the model substrates acetoacetyl-CoA or acetoacetyl-N-acetylcysteamine
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
Arg187 and Arg230 are critical residues for the FabG-acyl-carrier protein interactions, significance of the positively charged/hydrophobic patch located adjacent to the active site cavities of FabG for interactions with acyl carrier protein
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
-
-
-
r
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
?
additional information
?
-
-
animals, yeast and Mycobacteria have fatty acid synthetase containing all the individual activities on one or two multifunctional polypeptide chains, plants and most bacterial systems, including E. coli, possess individual monofunctional enzymes and a separate acyl carrier protein
-
-
-
additional information
?
-
-
beta-ketoacyl thioesters of CoA and pantetheine metabolized at slower rates
-
-
-
additional information
?
-
-
equally active on beta-ketoacyl-ACP derivatives of C4 to C16
-
-
-
additional information
?
-
-
broad specificity for chain length of substrates
-
-
-
additional information
?
-
-
broad specificity for chain length of substrates
-
-
-
additional information
?
-
-
catalyzes also the reduction of the beta-keto group of unsaturated acyl chains during biosynthesis of unsaturated fatty acids
-
-
-
additional information
?
-
-
FabG1 is responsible for the first reductive step of the fatty acid synthetic cycle. FabG2 is inactive in fatty acid synthesis
-
-
-
additional information
?
-
FabG1 is able to act on shorter (C4) acyl substrates
-
-
-
additional information
?
-
FabG1 is able to act on shorter (C4) acyl substrates
-
-
-
additional information
?
-
FabG1 is able to act on shorter (C4) acyl substrates
-
-
-
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
no activity with NADH
-
-
-
additional information
?
-
-
animals, yeast and Mycobacteria have fatty acid synthetase containing all the individual activities on one or two multifunctional polypeptide chains, plants and most bacterial systems, including E. coli, possess individual monofunctional enzymes and a separate acyl carrier protein
-
-
-
additional information
?
-
-
the beta-ketoacyl acyl carrier protein reductase activity of the fatty acid biosynthetic pathway is a determining factor of 3-oxo-homoserine lactone acyl chain lengths
-
-
-
additional information
?
-
-
the enzyme is essential in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa
-
-
-
additional information
?
-
fabG overexpression tends to depress the biosynthesis of medium-chain-length polyhydroxyalkanoate due to the reversible conversion of (R)-3-hydroxyalkanoate monomer units into 3-ketoacyl-CoA
-
-
-
additional information
?
-
-
fabG overexpression tends to depress the biosynthesis of medium-chain-length polyhydroxyalkanoate due to the reversible conversion of (R)-3-hydroxyalkanoate monomer units into 3-ketoacyl-CoA
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
beta-oxidation pathway
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme is part of the dissociable fatty acid synthase type II multienzyme complex for de novo synthesis of fatty acids from acetyl-CoA and malonyl-CoA
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
r
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
acetoacetyl-CoA + NADPH + H+
3-hydroxybutyryl-CoA + NADP+
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
-
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
?
additional information
?
-
-
catalyzes also the reduction of the beta-keto group of unsaturated acyl chains during biosynthesis of unsaturated fatty acids
-
-
-
additional information
?
-
-
FabG1 is responsible for the first reductive step of the fatty acid synthetic cycle. FabG2 is inactive in fatty acid synthesis
-
-
-
additional information
?
-
-
the beta-ketoacyl acyl carrier protein reductase activity of the fatty acid biosynthetic pathway is a determining factor of 3-oxo-homoserine lactone acyl chain lengths
-
-
-
additional information
?
-
-
the enzyme is essential in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa
-
-
-
additional information
?
-
fabG overexpression tends to depress the biosynthesis of medium-chain-length polyhydroxyalkanoate due to the reversible conversion of (R)-3-hydroxyalkanoate monomer units into 3-ketoacyl-CoA
-
-
-
additional information
?
-
-
fabG overexpression tends to depress the biosynthesis of medium-chain-length polyhydroxyalkanoate due to the reversible conversion of (R)-3-hydroxyalkanoate monomer units into 3-ketoacyl-CoA
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative cofactor binding
NADPH
exhibits negative cooperativity for its interaction with the enzyme
NADPH
-
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative allosteric cofactor binding in presence of [acyl-carrier-protein]
NADPH
-
3fold enhancement in acyl-carrier protein binding to wild-type in the presence of NADPH
additional information
-
NADH is used by NADH-dependent 3-oxoacyl [ACP]-reductase, EC 1.1.1.121
-
additional information
-
NADH is used by NADH-dependent 3-oxoacyl [ACP]-reductase, EC 1.1.1.121
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme activity is maximal at a ionic strength of 325 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one
80% residual activity
(E)-3-phenoxybenzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
61% residual activity
(E)-benzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
71% residual activity
(E)-phenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
69% residual activity
4-acetoxyanthecotulide
-
most active linear sesquiterpene lactone from Anthemis auriculata against FabG
4-hydroxyanthecotulide
-
linear sesquiterpene lactone from Anthemis auriculata
Acyl carrier protein
-
beta-ketobutyryl-CoA reductase activity of FabG1 is inhibited, activity of FabG2 is unaffected
acyl-carrier protein
-
inhibition of wild-type with increasing concentrations
anthecotulide
-
linear sesquiterpene lactone from Anthemis auriculata
bromochlorophen
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM
di-resorcinol sulfide
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM
grape skin extract
-
inhibits the overall reaction and beta-ketoacyl reductase reaction of FAS with IC50 values of 4.61 microg/ml and 20.3 microg/ml, respectively. Inhibits the overall reaction of FAS competitively with acetyl-CoA, noncompetitively with malonyl-CoA and in a mixed manner with NADPH
-
Guanidinium chloride
-
FabG is fully unfolded at 4 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. In presence of NADPH, there is no stabilization of FabG in case of equilibrium unfolding with guanidinium chloride
Hexachlorophene
an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
69% residual activity
resveratrol
-
inhibits the overall reaction and beta-ketoacyl reductase reaction of FAS with IC50 values of 11.1 microg/ml and 21.9 microg/ml, respectively. In 3 T3-L1 preadipocytes, resveratrol reduces lipid accumulation remarkably
RNAi
-
suppresses KCR activity, which results in a reduction of cuticular wax load and affects very-long-chain fatty acid composition of sphingolipids, seed triacylglycerols, and root glycerolipids. RNAi-suppressed Arabidopsis KCR1 plants display fused vegetative and reproductive organs, an abnormal root morphology and have abnormal trichome and epidermal cell morphology
-
Urea
-
FabG is fully unfolded at 6 M, approximately 90% of the enzyme activity can be recovered on dialyzing the denaturant. Two states in the reversible unfolding process of FabG in presence of NADPH, one is an activity-enhanced state and the other, an inactive state in case of equilibrium unfolding with urea
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
-
mixed type of inhibition. IC50 value 0.9 microgramm per ml, Ki value 0.21 microgramm per ml
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
-
compound is transported across cancer cell membrane to further down-regulate FAS and activate caspase-3 in MDA-MB-231 cells. Compared with other FAS inhibitors, including catechin gallate and morin, 1,2,3,4,6-penta-O-galloyl-beta-D-glucose involves a higher reversible fast-binding inhibition with an irreversible slow-binding inhibition, i.e. saturation kinetics with a dissociation constant of 0.59 microM and a limiting rate constant of 0.16 per min. The major reacting site of PGG is on the beta-ketoacyl reduction domain of FAS. Compound exhibits different types of inhibitions against the three substrates in the FAS overall reaction
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
-
minimal inhibitory concentration 0.125 mg/ml
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
-
minimal inhibitory concentration 0.25 mg/ml
Phenylglyoxal
-
with NADPH 45% remaining activity, without total loss of activity
Tannic acid
-
; strongest inhibition on FabG, shows time-dependent irreversible inhibition
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
cinnamic acid derivatives can be accommodated in the substrate-binding region of the active site, above the nicotinamide moiety of the NADPH cofactor
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge; inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge. Leaf extracts of Acer saccharum and Acer truncatum Bunge display time-dependent irreversible inhibition of FabG, whereas leaf extracts of Acer platanoides, Acer campestre and Acer rubrum show reversible inhibition
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge. Is inhibited by the leaf extracts from all five kinds of maples more effectively than are other Gram-negative bacteria strains
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is above 1.28 mM
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge. Is inhibited by the leaf extracts from all five kinds of maples more effectively than are other Gram-negative bacteria strains
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge. Is inhibited by the leaf extracts from all five kinds of maples more effectively than are other Gram-negative bacteria strains
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is 0.32-0.64 mM
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
-
additional information
-
inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge, except strain 04-5
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is 0.01-0.02 mM
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is 0.025-0.05 mM
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum), strongest inhibition with 40% ethanol extract of galangal. Inhibition is consisted of both reversible and irreversible inhibition. Inhibits FabG in a competitive pattern against NADPH, irreversible inhibition presents two phases (slow and fast one)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
affinity of acyl-carrier protein for FabG is increased by 3fold in the presence of 1 M urea
-
additional information
variation of the buffer molarity between 25 mM and 200 mM or addition of NaCl up to 500 mM has no significant effect on enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Inhibition of M. tuberculosis ?-ketoacyl CoA reductase FabG4 (Rv0242c) by triazole linked polyphenol-aminobenzene hybrids: Comparison with the corresponding gallate counterparts.
Infections
Novel Xanthomonas campestris Long-Chain-Specific 3-Oxoacyl-Acyl Carrier Protein Reductase Involved in Diffusible Signal Factor Synthesis.
Polycystic Kidney Diseases
A C. elegans model for mitochondrial fatty acid synthase II: the longevity-associated gene W09H1.5/mecr-1 encodes a 2-trans-enoyl-thioester reductase.
Tuberculosis
Crystal structure of FabG4 from Mycobacterium tuberculosis reveals the importance of C-terminal residues in ketoreductase activity.
Tuberculosis
Crystal structure of hexanoyl-CoA bound to ?-ketoacyl reductase FabG4 of Mycobacterium tuberculosis.
Tuberculosis
Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH.
Tuberculosis
Design, synthesis and characterization of dual inhibitors against new targets FabG4 and HtdX of Mycobacterium tuberculosis.
Tuberculosis
Design, synthesis and characterization of novel inhibitors against mycobacterial ?-ketoacyl CoA reductase FabG4.
Tuberculosis
Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG but not Escherichia coli fabG.
Tuberculosis
In vitro inhibition of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA by isoniazid.
Tuberculosis
Inhibition of M. tuberculosis ?-ketoacyl CoA reductase FabG4 (Rv0242c) by triazole linked polyphenol-aminobenzene hybrids: Comparison with the corresponding gallate counterparts.
Tuberculosis
Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change.
Tuberculosis
Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding.
Tuberculosis
Novel katG mutations causing isoniazid resistance in clinical M. tuberculosis isolates.
Tuberculosis
Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis.
Tuberculosis
Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
89.2
1,1,1-trifluoroacetone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
5.72
2',3',4',5',6'-pentafluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
7.38
3'-fluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
14.34
4'-chloroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
12.29
4'-fluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
46.92
acetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2.71
alpha-chloroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
8.31
ethyl 4-chloroacetoacetate
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.92
ethylbenzoylacetate
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.29
NADP+
with 3-hydroxydecanoyl-N-acetylcysteamine as cosubstrate, pH and temperature not specified in the publication
6.03
propiophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.8871
acetoacetyl-CoA
mutant enzyme S36A, at pH 8.0 and 25°C
0.9913
acetoacetyl-CoA
mutant enzyme S40A, at pH 8.0 and 25°C
1
acetoacetyl-CoA
pH and temperature not specified in the publication
0.29
NADPH
with acetoacetyl-CoA as cosubstrate, pH and temperature not specified in the publication
additional information
additional information
kinetic analysis of the recombinant enzyme, kinetic mechanism
-
additional information
additional information
-
detailed steady-state kinetic analysis, solvent and multiple kinetic isotope effects, random bi bi kinetic mechanism
-
additional information
additional information
-
detailed kinetic and thermodynamic analysis, solvent and multiple kinetic isotope effects, kinetic mechanism
-
additional information
additional information
-
cooperativity kinetics, binding constants of substrates and cofactors
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
product inhibition kinetics, overview
-
additional information
additional information
-
inhibition kinetic analysis
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0154
bromochlorophen
Plasmodium falciparum
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM
0.0038
di-resorcinol sulfide
Plasmodium falciparum
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM
0.002
Hexachlorophene
Plasmodium falciparum
an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM
0.215
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
Escherichia coli
pH 7.0
additional information
grape skin extract
Gallus gallus
-
IC50 value is 20.3 microg/ml, pH 7.0, 37°C
-
additional information
additional information
synthetic construct
-
IC(50) value of 4.47 microg/ml for extract of galangal, pH 7.0
-
additional information
resveratrol
Gallus gallus
-
IC50 value is 21.9 microg/ml, pH 7.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
with 2-octanone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.08
with 4'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.13
with 3'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0; with acetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.15
with 4'-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.16
with propiophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.44
mutant enzyme R34A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C; mutant enzyme R34A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
0.46
mutant enzyme K152A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
0.5
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
0.85
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
1.03
with 1,1,1-trifluoroacetone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.16
with ethylbenzoylacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.2
mutant enzyme K173A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
1.3
mutant enzyme K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
1.6
mutant enzyme R168E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
1.7
mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
136000
-
purified enzyme, protein determination by calculation from absorption at 280 nm
14.8
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
15.7
mutant enzyme K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
17.4
mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
2.45
with alpha-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2.6
wild type enzyme, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
20.7
mutant enzyme R34A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
20.8
wild type enzyme, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
25.5
mutant enzyme K152A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
3
-
mutant R187A/R230A, acyl-carrier protein-dependent spectroscopic assay
3.1
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
3.93
with 2',3',4',5',6'-pentafluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
31.8
mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
38.29
with ethyl 4-chloroacetoacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
4.3
mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
4.5
mutant enzyme K173A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
42.6
-
mutant R187E/R230E, acyl-carrier protein-independent spectroscopic assay
45.6
-
mutant R187A/R230A, acyl-carrier protein-independent spectroscopic assay
5.4
mutant enzyme D42A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
54.2
-
mutant R230E, acyl-carrier protein-independent spectroscopic assay
54.5
-
mutant R187E, acyl-carrier protein-independent spectroscopic assay
55.3
-
mutant R230A, acyl-carrier protein-independent spectroscopic assay
57.9
-
mutant R187A, acyl-carrier protein-independent spectroscopic assay
59.8
6.3
7.9
mutant enzyme R168E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
74.6
mutant enzyme D42A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
8.4
mutant enzyme Q126E/R168E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
additional information
2
-
mutant R187E/R230E, acyl-carrier protein-dependent spectroscopic assay
additional information
the intrinsic NADPH dependent 3-ketoacyl-CoA reductase activity in the transformant Pseudomonas putida with overexpressed fabG gene increased about 1.6-fold from 0.87 to 1.39 units/mg protein, indicating successful overexpression of the fabGJ genes in Pseudomonas putida KCTC1639.
additional information
-
the intrinsic NADPH dependent 3-ketoacyl-CoA reductase activity in the transformant Pseudomonas putida with overexpressed fabG gene increased about 1.6-fold from 0.87 to 1.39 units/mg protein, indicating successful overexpression of the fabGJ genes in Pseudomonas putida KCTC1639.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
additional information
-
increase in alpha-secondary deuterium kinetic isotope effect values measured at pH 10 as compared to those obtained at pH 7 points to isotope- and pH-sensitive steps occurring concomitantly
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
pH 4: about 60% of maximal activity, pH 10: about 75% of maximal activity
5.5 - 9.5
-
pH profile, detailed mechanistic pH-dependence analysis, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
30°C: about 55% of maximal activity, 55°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 61-3, non-pathogenic strain from soil, gene fabG
SwissProt
brenda
alpha-haemolytic strain 32213-7 and beta-haemolytic strain 32210-20
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
loss of KCR1 function results in embryo lethality, which cannot be rescued by KCR2 expression using the KCR1 promoter. Disruption of the KCR2 gene has no obvious phenotypic effect
malfunction
-
DELTAfabG1 cells lose the ability to accumulate poly(3-hydroxybutyrate-co-3-hydroxyvalerate). When the DELTAfabG1 strain is transformed with the fabG1 expression plasmid pWLG1, the capability of polyhydroxyalkanoate accumulation is restored. When the fabG1 gene is disrupted or knocked out, the NADPH-dependent activity of acetoacetyl-CoA reductase in the mutant, the DELTAfabG1 or fabG1-1 strain, is greatly decreased
malfunction
-
DELTAfabG1 cells lose the ability to accumulate poly(3-hydroxybutyrate-co-3-hydroxyvalerate). When the DELTAfabG1 strain is transformed with the fabG1 expression plasmid pWLG1, the capability of polyhydroxyalkanoate accumulation is restored. When the fabG1 gene is disrupted or knocked out, the NADPH-dependent activity of acetoacetyl-CoA reductase in the mutant, the DELTAfabG1 or fabG1-1 strain, is greatly decreased
-
physiological function
-
only KCR1 is a functional KCR isoform involved in microsomal fatty acid elongation
physiological function
-
FabG1 has the function of supplying precursors for polyhydroxyalkanoate biosynthesis
physiological function
-
FabG1 has the function of supplying precursors for polyhydroxyalkanoate biosynthesis
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aquifex aeolicus (strain VF5)
Bacillus subtilis (strain 168)
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Brucella abortus (strain 2308)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Brucella suis (strain ATCC 23445 / NCTC 10510)
Burkholderia multivorans (strain ATCC 17616 / 249)
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Escherichia coli (strain K12)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Paraburkholderia xenovorans (strain LB400)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Rhizobium meliloti (strain 1021)
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Synechococcus elongatus (strain PCC 7942)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
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 tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
116000
-
recombinant enzyme, analytical ultracentrifugation, tetrameric at higher enzyme concentrations
24000
25000
25500
28000
29000
-
2 * 29000, recombinant enzyme, SDS-PAGE; 4 * 29000, SDS-PAGE, tetrameric at higher enzyme concentrations
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE