Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.1.1.100
-
RECOMMENDED NAME
GeneOntology No.
3-oxoacyl-[acyl-carrier-protein] reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
belongs to family of short-chain alcohol dehydrogenases (SDR) with catalytic triad Ser154, Tyr167 and Lys171, catalytic mechanism
-
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
ordered bi bi kinetic mechanism, [acyl-carrier protein] recognition mechanism
Q86RB1
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
reaction mechanism, random bi bi kinetic mechanism
-
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
chemical and kinetic mechanism
-
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
cofactor and substrate binding kinetics, allosteric regulation mechanism, overview
-
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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
-
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
redox reaction
A5HIF6, -
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
8-amino-7-oxononanoate biosynthesis I
-
Biosynthesis of unsaturated fatty acids
-
Biotin metabolism
-
cis-dodecenoyl biosynthesis
-
cis-vaccenate biosynthesis
-
docosahexanoate biosynthesis I
-
docosahexanoate biosynthesis II
-
Fatty acid biosynthesis
-
fatty acid elongation -- saturated
-
Metabolic pathways
-
mycolate biosynthesis
-
octanoyl-ACP biosynthesis (mitochondria, yeast)
-
palmitate biosynthesis I (animals and fungi)
-
palmitate biosynthesis II (bacteria and plants)
-
palmitoleate biosynthesis I
-
petroselinate biosynthesis
-
stearate biosynthesis II (bacteria and plants)
-
stearate biosynthesis III (fungi)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-ketoacyl acyl carrier protein reductase
-
-
-
-
3-ketoacyl-(acyl-carrier-protein) reductase
P50941
-
3-ketoacyl-ACP reductase
A5HIF6
-
3-ketoacyl-ACP(CoA) reductase
-
-
3-ketoacyl-acyl carrier protein reductase
-
-
-
-
3-ketoacyl-acyl carrier protein reductase
-
-
3-ketoacyl-acyl carrier protein reductase
A5HIF6
-
3-ketoacyl-acyl carrier protein reductase
Q4AE87
-
3-ketoacyl-[acyl-carrier-protein] reductase
Q31QF3
-
3-oxoacyl-(acyl carrier protein) reductase
Q81JG6
-
3-oxoacyl-ACP reductase
Q86RB1
-
3-oxoacyl-ACP reductase
-
-
3-oxoacyl-AcpM reductase
O53665, P0A5Y4
-
3-oxoacyl-thioester reductase
-
-
3-oxoacyl-thioester reductase
-
-
3-oxoacyl-[ACP]reductase
-
-
-
-
beta-ketoacyl acyl carrier protein (ACP) reductase
-
-
-
-
beta-ketoacyl acyl carrier protein reductase
-
-
beta-ketoacyl acyl carrier protein reductase
-
-
beta-ketoacyl reductase
-
-
-
-
beta-ketoacyl reductase
-
-
beta-ketoacyl reductase
-
-
beta-ketoacyl reductase
-
-
beta-ketoacyl thioester reductase
-
-
-
-
beta-ketoacyl-ACP reductase
-
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Acinetobacter calcoaceticus 25001
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Enterobacter aerogenes 45102
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Enterobacter cloacae 45301
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Pseudomonas aeruginosa ATCC27853
-
-
-
beta-ketoacyl-ACP reductase
Salmonella enterica subsp. enterica serovar Typhi H901
-
-
-
beta-ketoacyl-ACP reductase
Serratia marcescens 41002
-
-
-
beta-ketoacyl-ACP reductase
Shigella sonnei 51592
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
Staphylococcus aureus ATCC25923
-
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-ACP reductase
-
-
beta-ketoacyl-acyl carrier protein reductase
-
-
-
-
beta-ketoacyl-acyl carrier protein reductase
-
-
beta-ketoacyl-acyl carrier protein reductase
-
-
beta-ketoacyl-acyl carrier protein reductase
-
-
beta-ketoacyl-[acyl carrier protein] reductase
-
-
beta-ketoacyl-[acyl-carrier protein] (ACP) reductase
-
-
-
-
FabG
Acinetobacter calcoaceticus 25001
-
-
-
FabG
Enterobacter aerogenes 45102
-
-
-
FabG
Enterobacter cloacae 45301
-
-
-
FabG
Pseudomonas aeruginosa ATCC27853
-
-
-
FabG
A5HIF6
-
FabG
Q4AE87
-
FabG
P50941
gene name
FabG
Salmonella enterica subsp. enterica serovar Typhi H901
-
-
-
FabG
Serratia marcescens 41002
-
-
-
FabG
Shigella sonnei 51592
-
-
-
FabG
Staphylococcus aureus ATCC25923
-
-
-
FabG1
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
-
-
NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
-
-
-
-
PHA-specific acetoacetyl-CoA reductase
-
-
PHA-specific acetoacetyl-CoA reductase
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
-
-
PHA-specific acetoacetyl-CoA reductase
-
-
PhaB
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
-
-
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
-
-
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
-
-
polyhydroxyalkanoate-specific acetoacetyl coenzyme A reductase
-
-
reductase, 3-oxoacyl-[acyl carrier protein]
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37250-34-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acinetobacter calcoaceticus 25001
strain 25001
-
-
Manually annotated by BRENDA team
isoform FabG
-
-
Manually annotated by BRENDA team
rapeseed
-
-
Manually annotated by BRENDA team
strain 45102
-
-
Manually annotated by BRENDA team
Enterobacter aerogenes 45102
strain 45102
-
-
Manually annotated by BRENDA team
strain 45301
-
-
Manually annotated by BRENDA team
Enterobacter cloacae 45301
strain 45301
-
-
Manually annotated by BRENDA team
strains ATCC29212 and 775
-
-
Manually annotated by BRENDA team
; strains ATCC 25922 and 26
-
-
Manually annotated by BRENDA team
strain AS2049
-
-
Manually annotated by BRENDA team
Haloarcula hispanica AS2049
strain AS2049
-
-
Manually annotated by BRENDA team
strains ATCC700603 and 14
-
-
Manually annotated by BRENDA team
ssp. lactis IL 1403
-
-
Manually annotated by BRENDA team
avocado
-
-
Manually annotated by BRENDA team
gene fabG
SwissProt
Manually annotated by BRENDA team
gene fabG, no isozymes
-
-
Manually annotated by BRENDA team
strains ATCC27853 and 17
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa ATCC27853
ATCC27853
-
-
Manually annotated by BRENDA team
strain 61-3, non-pathogenic strain from soil, gene fabG
SwissProt
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhi H901
strain H901
-
-
Manually annotated by BRENDA team
strain 41002
-
-
Manually annotated by BRENDA team
Serratia marcescens 41002
strain 41002
-
-
Manually annotated by BRENDA team
strain 51592
-
-
Manually annotated by BRENDA team
Shigella sonnei 51592
strain 51592
-
-
Manually annotated by BRENDA team
strains ATCC29213, 15 and 05-3
-
-
Manually annotated by BRENDA team
Staphylococcus aureus ATCC25923
ATCC25923
-
-
Manually annotated by BRENDA team
strains ATCC12228, 04-5 and 05-1
-
-
Manually annotated by BRENDA team
alpha-haemolytic strain 32213-7 and beta-haemolytic strain 32210-20
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
polyhydroxyalkanoate-defective haloarchaeon
malfunction
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
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
Haloarcula hispanica AS2049, Haloarcula hispanica CGMCC1.2049
-
FabG1 has the function of supplying precursors for polyhydroxyalkanoate biosynthesis
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
A5HIF6, -
beta-oxidation pathway
-
-
?
1,1,1-trifluoroacetone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
792% relative activity compared to acetophenone
-
-
?
2',3',4',5',6'-pentafluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
3023% relative activity compared to acetophenone
-
-
?
2-octanone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
15% relative activity compared to acetophenone
-
-
?
3'-fluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
100% relative activity compared to acetophenone
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
-
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
Euglena gracilis Z
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-, cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding
-
-
r
4'-chloroacetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
115% relative activity compared to acetophenone
-
-
?
4'-fluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
62% relative activity compared to acetophenone
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
P0AEK2
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
r
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
Q965D6
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-, Q4AE87
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
Q86RB1
-
-
-
?
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
? + NADP+
show the reaction diagram
-
wild-type shows less activity with acetoacetyl-CoA than with acetoacetyl-[acyl-carrier protein]
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
-
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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
-
-
?
acetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
100% relative activity
-
-
?
alpha-chloroacetophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
1885% relative activity compared to acetophenone
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
beta-ketobutyryl-CoA + NADPH
beta-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
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
-
-
-
crotonyl-CoA + NADPH
?
show the reaction diagram
-
-
-
-
?
dec-2-enoyl-CoA + NADPH
3-hydroxydecanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
dec-2-enoyl-CoA + NADPH
3-hydroxydecanoyl-CoA + NADP+
show the reaction diagram
Q4AE87
-
-
-
?
dodec-2-enoyl-CoA + NADPH
3-hydroxydodecanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
dodec-2-enoyl-CoA + NADPH
3-hydroxydodecanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
dodec-2-enoyl-CoA + NADPH
3-hydroxydodecanoyl-CoA + NADP+
show the reaction diagram
-, Q4AE87
-
-
-
?
ethyl 4-chloroacetoacetate + NADPH
? + NADP+
show the reaction diagram
Q31QF3
29454% relative activity compared to acetophenone
-
-
?
ethyl acetoacetate + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
ethyl acetoacetate + NADPH
ethyl 3-hydroxybutyrate + NADP+
show the reaction diagram
-
-
-
-
?
ethyl acetoacetate + NADPH
ethyl 3-hydroxybutyrate + NADP+
show the reaction diagram
-
-
-
-
?
ethylbenzoylacetate + NADPH
? + NADP+
show the reaction diagram
Q31QF3
892% relative activity compared to acetophenone
-
-
?
hex-2-enoyl-CoA + NADPH
3-hydroxyhexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
hex-2-enoyl-CoA + NADPH
3-hydroxyhexanoyl-CoA + NADP+
show the reaction diagram
Q4AE87
-
-
-
?
oct-2-enoyl-CoA + NADPH
3-hydroxyoctanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
oct-2-enoyl-CoA + NADPH
3-hydroxyoctanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
oct-2-enoyl-CoA + NADPH
3-hydroxyoctanoyl-CoA + NADP+
show the reaction diagram
-, Q4AE87
-
-
-
?
propiophenone + NADPH
? + NADP+
show the reaction diagram
Q31QF3
123% relative activity compared to acetophenone
-
-
?
propyl acetoacetate + NADPH
? + NADP+
show the reaction diagram
-
as substrate it is limited to its weak solubility
-
-
?
methyl acetoacetate + NADPH
? + NADP+
show the reaction diagram
-
is not a good substrate as ethyl acetoacetate
-
-
?
additional information
?
-
-
only D-(-) isomer is oxidized, beta-ketoacyl thioesters of CoA and pantetheine metabolized at slower rates
-
-
-
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
?
-
-
equally active on beta-ketoacyl-ACP derivatives of C4 to C16, broad specificity for chain length of substrates
-
-
-
additional information
?
-
-
broad specificity for chain length of substrates
-
-
-
additional information
?
-
-
L-isomer completely inactive
-
-
-
additional information
?
-
-
L-isomer completely inactive
-
-
-
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
?
-
-
the enzyme is part of the fatty acid synthase multienzyme complex, and shares probably a single active site with the enoyl reductase activity of the complex
-
-
-
additional information
?
-
-
FabG substrate specificity overview
-
-
-
additional information
?
-
Q4AE87
FabG substrate specificity overview
-
-
-
additional information
?
-
A5HIF6, -
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
?
-
O53665, P0A5Y4
FabG1 is able to act on shorter (C4) acyl substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
A5HIF6, -
beta-oxidation pathway
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
first reduction step of fatty acid synthase
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
enzyme in fatty acid synthesis
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
r
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
-
first reductive step in the elongation cycle of fatty acid biosynthesis
-
-
?
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
?
-
-
the enzyme is part of the fatty acid synthase multienzyme complex, and shares probably a single active site with the enoyl reductase activity of the complex
-
-
-
additional information
?
-
A5HIF6, -
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADH
-
NADPH is much more effective than NADH
NADP+
-
cooperative transitions in the enzyme due to cofactor and [acyl-carrier-protein] binding, cooperative cofactor binding
NADPH
-
absolute specificity for NADPH
NADPH
-
much more effective than NADH
NADPH
-
absolute specificity for NADPH
NADPH
-
absolute specificity for NADPH
NADPH
Q965D6
exhibits negative cooperativity for its interaction with the enzyme
NADPH
Q86RB1
cofactor binding structure and mechanism
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
-
positive cooperativity in binding to enzyme
NADPH
-
dependent on
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
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q86RB1
the enzyme activity is maximal at a ionic strength of 325 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one
P0AEK2
80% residual activity
(E)-2-nitrophenyl cinnamate
P0AEK2
-
(E)-3-phenoxybenzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
61% residual activity
(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
-
(E)-benzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
71% residual activity
(E)-phenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
69% residual activity
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
-
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
3-hydroxybutyryl-CoA
Q86RB1
competitive product inhibition
3-hydroxybutyryl-CoA
-
noncompetitive product inhibition pattern
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
Bithionol
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.010 mM
bromochlorophen
Q86RB1
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM
chlorogenic acid
-
IC50: 0.881-0.948 mM
di-resorcinol sulfide
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM
DL-3-hydroxybutyryl-CoA
-
competitive product inhibition
epigallocatechin gallate
-
-
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
Q86RB1
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
P0AEK2
69% residual activity
NADP+
-
competitive product inhibition
NADP+
-
noncompetitive product inhibition pattern
NADP+
-
competitive product inhibition
p-chloromercuribenzoate
-
-
Phenylglyoxal
-
with NADPH 45% remaining activity, without total loss of activity
Phenylglyoxal
-
-
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
-
Tannic acid
-
; strongest inhibition on FabG, shows time-dependent irreversible inhibition
Tannic acid
-
displays very strong inhibition
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
additional information
-
not: N-ethylmaleimide, arsenite
-
additional information
Q86RB1
no inhibition by triclosan
-
additional information
P0AEK2
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
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is above 1.28 mM
-
additional information
-
FabG is inhibited by extract of galangal (rhizome of Alpinia officinarum). Minimum inhibitory concentration is 0.32-0.64 mM
-
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)
-
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; 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. 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. 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. 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, except strain 04-5
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
Q31QF3
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
-
additional information
-
affinity of acyl-carrier protein for FabG is increased by 3fold in the presence of 1 M urea
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
89.2
-
1,1,1-trifluoroacetone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
5.72
-
2',3',4',5',6'-pentafluoroacetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
7.38
-
3'-fluoroacetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
14.34
-
4'-chloroacetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
12.29
-
4'-fluoroacetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.0012
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant mutant K1699Q
0.002
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant mutant K1699A
0.01
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant wild-type enzyme
0.075
-
acetoacetyl-CoA
Q965D6
pH 7.5
0.165
-
acetoacetyl-CoA
-
pH 7.6, 30C
0.25
-
acetoacetyl-CoA
-
-
0.261
-
acetoacetyl-CoA
-
-
0.43
-
acetoacetyl-CoA
-
pH 6.8, 22C, recombinant enzyme
0.43
-
acetoacetyl-CoA
-
wild-type
0.44
-
acetoacetyl-CoA
-
mutant R230A
0.45
-
acetoacetyl-CoA
-
mutant R187A
0.47
-
acetoacetyl-CoA
-
-
0.47
-
acetoacetyl-CoA
-
mutant R187A/R230A; mutant R187E
0.49
-
acetoacetyl-CoA
-
mutant R230E
0.51
-
acetoacetyl-CoA
Q86RB1
pH 6.8, 25C, recombinant enzyme
0.58
-
acetoacetyl-CoA
-
mutant R187E/R230E
2.2
-
acetoacetyl-CoA
-
pH 7.6, 30C
48
-
acetoacetyl-N-acetylcysteamine
-
-
0.003
-
acetoacetyl-[acyl-carrier protein]
-
-
0.0037
-
acetoacetyl-[acyl-carrier protein]
-
-
0.0079
-
acetoacetyl-[acyl-carrier protein]
-
-
0.009
-
acetoacetyl-[acyl-carrier protein]
-
-
0.017
-
acetoacetyl-[acyl-carrier protein]
-
-
46.92
-
acetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2.71
-
alpha-chloroacetophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.29
-
beta-ketobutyryl-CoA
-
pH 7.0, 30C, FabG1
4.06
-
beta-ketobutyryl-CoA
-
pH 7.0, 30C, FabG2
0.006
-
crotonyl-CoA
-
pH 7.4, 25C, recombinant wild-type enzyme
0.007
-
dodecenoyl-CoA
-
pH 7.4, 25C, recombinant wild-type enzyme
-
8.31
-
ethyl 4-chloroacetoacetate
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.127
-
ethyl acetoacetate
-
-
0.035
-
N-acetoacetyl-N-cysteamine
-
-
-
0.003
-
NADPH
-
pH 7.4, 25C, recombinant wild-type enzyme, with crotonyl-CoA
0.005
-
NADPH
-
pH 7.4, 25C, recombinant wild-type enzyme, with acetoacetyl-CoA
0.0093
-
NADPH
-
-
0.01
-
NADPH
-
-
0.015
-
NADPH
-
-
0.023
-
NADPH
-
+ acetoacetyl-[acyl-carrier-protein]
0.025
-
NADPH
-
-
0.026
-
NADPH
-
pH 7.6, 30C
0.0412
-
NADPH
-
in the presence of 1.5 M urea, pH 7.0, 25C
0.043
-
NADPH
-
pH 6.8, 22C, recombinant enzyme
0.0434
-
NADPH
-
in the presence of 1 M urea, pH 7.0, 25C
0.0461
-
NADPH
-
without urea, pH 7.0, 25C
0.0475
-
NADPH
Q86RB1
pH 6.8, 25C, recombinant enzyme
0.052
-
NADPH
-
pH 7.4, 25C, recombinant mutant K1699A, with acetoacetyl-CoA
0.1
-
NADPH
-
pH 7.4, 25C, recombinant wild-type enzyme, with octenoyl-CoA
0.123
-
NADPH
-
pH 7.4, 25C, recombinant mutant K1699Q, with acetoacetyl-CoA
0.4
-
NADPH
-
pH 7.6, 30C
0.4553
-
NADPH
-
in the presence of 4 M urea, pH 7.0, 25C
0.54
-
NADPH
-
pH 7.4, 25C, recombinant wild-type enzyme, with dodecenoyl-CoA
6.03
-
propiophenone
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.92
-
ethylbenzoylacetate
Q31QF3
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Q86RB1
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.014
-
acetoacetyl-CoA
Q965D6
pH 7.5
0.33
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant mutant K1699A
0.43
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant mutant K1699Q
4
-
acetoacetyl-CoA
-
pH 7.4, 25C, recombinant wild-type enzyme
7
-
acetoacetyl-CoA
-
pH 7.0, 25C
11
-
acetoacetyl-CoA
-
pH 7.6, 30C
259
-
acetoacetyl-CoA
-
pH 6.8, 22C, recombinant enzyme
265
-
acetoacetyl-CoA
Q86RB1
pH 6.8, 25C, recombinant enzyme
0.3
-
ethyl acetoacetate
-
-
0.33
-
NADPH
-
pH 7.4, 25C, recombinant mutant K1699A
0.43
-
NADPH
-
pH 7.4, 25C, recombinant mutant K1699Q
0.59
-
NADPH
-
-
4
-
NADPH
-
pH 7.4, 25C, recombinant wild-type enzyme
7
-
NADPH
-
pH 7.6, 30C
11
-
NADPH
-
pH 7.6, 30C
148.6
-
NADPH
-
in the presence of 4 M urea, pH 7.0, 25C
187.3
-
NADPH
-
in the presence of 1.5 M urea, pH 7.0, 25C
250
-
NADPH
-
without urea, pH 7.0, 25C
259
-
NADPH
-
pH 6.8, 22C, recombinant enzyme
265
-
NADPH
Q86RB1
pH 6.8, 25C, recombinant enzyme
344.7
-
NADPH
-
in the presence of 1 M urea, pH 7.0, 25C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0102
-
3-hydroxybutyryl-CoA
Q86RB1
pH 6.8, 25C, recombinant enzyme
additional information
-
additional information
-
product inhibition kinetics, overview
-
additional information
-
additional information
-
inhibition kinetic analysis
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.45
-
(E)-2-nitrophenyl cinnamate
P0AEK2
pH 7.0
0.18
-
(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
pH 7.0
0.18
-
(E)-phenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
P0AEK2
pH 7.0
0.5
-
4-acetoxyanthecotulide
-
pH 7.0, 25C
0.75
-
4-hydroxyanthecotulide
-
pH 7.0, 25C
1
-
anthecotulide
-
pH 7.0, 25C
0.01
-
Bithionol
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.010 mM
0.0154
-
bromochlorophen
Q86RB1
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM
0.881
0.948
chlorogenic acid
-
IC50: 0.881-0.948 mM
0.0038
-
di-resorcinol sulfide
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM
0.00554
-
epigallocatechin gallate
-
at pH 8.0
0.0084
-
epigallocatechin gallate
-
at pH 8.3
0.0105
-
epigallocatechin gallate
-
at pH 7.5
0.0336
-
epigallocatechin gallate
-
at pH 8.5
0.0578
-
epigallocatechin gallate
-
at pH 7.0
0.12
-
epigallocatechin gallate
-
at pH 9.0
0.1223
-
epigallocatechin gallate
-
at pH 6.5
0.002
-
Hexachlorophene
Q86RB1
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
P0AEK2
pH 7.0
0.3048
-
quercetin
-
pH 7.0
0.00078
-
Tannic acid
-
-
0.0212
-
kaempferol
-
pH 7.0
additional information
-
additional information
-
IC(50) value of 4.47 microg/ml for extract of galangal, pH 7.0
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0017
0.0018
-
recombinant refolded enzyme
0.0019
-
-
recombinant soluble enzyme
0.0032
-
-
-
0.0132
-
-
-
0.0168
-
-
-
0.0192
-
-
-
0.02
-
Q31QF3
with 2-octanone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.036
-
-
recombinant purified mutant K1699A
0.0366
-
-
-
0.043
-
-
recombinant purified mutant K1699Q
0.08
-
Q31QF3
with 4'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.13
-
Q31QF3
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
-
Q31QF3
with 4'-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.16
-
Q31QF3
with propiophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.24
-
-
recombinant purified wild-type BKR
1.03
-
Q31QF3
with 1,1,1-trifluoroacetone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.16
-
Q31QF3
with ethylbenzoylacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2
-
-
mutant R187E/R230E, acyl-carrier protein-dependent spectroscopic assay
2.45
-
Q31QF3
with alpha-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
3
-
-
mutant R187A/R230A, acyl-carrier protein-dependent spectroscopic assay
3.93
-
Q31QF3
with 2',3',4',5',6'-pentafluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
4
-
-
mutant R230E, acyl-carrier protein-dependent spectroscopic assay
6.1
-
-
mutant R230A, acyl-carrier protein-dependent spectroscopic assay
6.3
-
-
mutant R187E, acyl-carrier protein-dependent spectroscopic assay
6.9
-
-
mutant R187A, acyl-carrier protein-dependent spectroscopic assay
38.29
-
Q31QF3
with ethyl 4-chloroacetoacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
42.6
-
-
mutant R187E/R230E, acyl-carrier protein-independent spectroscopic assay
45.6
-
-
mutant R187A/R230A, acyl-carrier protein-independent spectroscopic assay
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
-
-
purified recombinant enzyme
59.8
-
-
wild-type, acyl-carrier protein-independent spectroscopic assay
70.6
-
-
wild-type, acyl-carrier protein-dependent spectroscopic assay
280
-
-
acetoacetyl-N-acetylcysteamine
450
-
-
acetoacetyl-CoA
530
-
-
acetoacteyl-ACP
3839
-
-
recombinant protein, cosubstrate NADH, pH 7.0, phosphate buffer
4930
-
-
purified enzyme
9401
-
-
purified enzyme, protein determination by amino acid analysis
83140
-
-
cosubstrate NADPH, pH 8.35, carbonate buffer
136000
-
-
purified enzyme, protein determination by calculation from absorption at 280 nm
180400
-
-
recombinant protein, cosubstrate NADPH, pH 7.0, phosphate buffer
additional information
-
-
-
additional information
-
A5HIF6, -
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.
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
Q86RB1
-
6.8
-
-
assay at
7
-
-
assay at
7
-
-
assay conditions
7.4
-
-
assay at
7.5
-
-
assay at
8
-
-
assay at
8
-
Q4AE87
assay at
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
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
Q31QF3
pH 4: about 60% of maximal activity, pH 10: about 75% of maximal activity
5.5
8.5
-
about 50% of activity maximum at pH 5.5 and 8.5
5.5
9.5
-
pH profile, detailed mechanistic pH-dependence analysis, overview
5.8
10
-
pH profile, pH-dependence analysis, overview
6
8.7
-
both reaction directions
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
22
-
Q4AE87
assay at room temperature
22
-
-
assay at room temperature
25
-
Q86RB1
assay at
25
-
-
assay at
30
-
A5HIF6, -
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
37
-
temperature profile
30
55
Q31QF3
30C: about 55% of maximal activity, 55C: about 65% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
A5HIF6, -
predicted
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q965D6
recombinant enzyme from Escherichia coli
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Acholeplasma laidlawii (strain PG-8A)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
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)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia pseudomallei (strain 1710b)
Cupriavidus taiwanensis (strain R1 / LMG 19424)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Plasmodium falciparum (isolate 3D7)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rhizobium meliloti (strain 1021)
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Rickettsia prowazekii (strain Madrid E)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Synechococcus elongatus (strain PCC 7942)
Synechococcus elongatus (strain PCC 7942)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 MJ-1236)
Vibrio cholerae serotype O1 (strain MJ-1236)
Vibrio cholerae serotype O1 (strain MJ-1236)
Vibrio cholerae serotype O1 (strain MJ-1236)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25500
-
A5HIF6, -
derived from amino acid sequence containing 246 amino acids
35000
-
-
sequence analysis, KCR2
40000
46000
-
gel filtration, sucrose density gradient centrifugation
44000
-
-
gel filtration
50400
-
-
recombinant enzyme, gel filtration
58400
-
-
recombinant enzyme, analytical ultracentrifugation
64000
-
-
gel filtration
97000
-
-
gel filtration
102000
-
Q31QF3
gel filtration
110000
-
-
gel filtration, wild-type and mutants
116000
-
-
recombinant enzyme, analytical ultracentrifugation, tetrameric at higher enzyme concentrations
120000
-
-
gel filtration
130000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
? * 27000, DNA sequence calculation
?
-
? * 24000, SDS-PAGE
?
Q965D6
x * 28000, SDS-PAGE
?
-
x * 24000, recombinant methionine-labelled FabG2, SDS-PAGE; x * 25000, recombinant methionine-labelled FabG1, SDS-PAGE
dimer
-
2 * 29000, recombinant enzyme, SDS-PAGE
tetramer
-
4 * 24200, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 20000-30000, SDS-PAGE
tetramer
-
4 * 28000, SDS-PAGE
tetramer
Q86RB1
crystal structure and ultrafiltration, quarternary structure analysis, monomer interactions, conformations in absence and presence of cofactor NADP+
tetramer
-
4 * 29000, SDS-PAGE, tetrameric at higher enzyme concentrations
tetramer
-
crystallization data
tetramer
Q31QF3
4 * 25500, SDS-PAGE
tetramer
-
cross-linking of native and up to 1 M urea-treated FabG
tetramer
-
crystallography
homotetramer
-
4 * 31000, SDS-PAGE, wild-type and mutants
additional information
-
animals, yeast and Mycobacteria have fatty acid synthetases containing all the individual activities on one or two multifunctional polypeptide chains, plants and most bacterial systems, including Escherichia coli, possess individual monofunctional enzymes and a separate acyl carrier protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
Q86RB1
the enzyme contains a signal peptide
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
diffraction to 1.8 A, determinantion of initial phases by molecular replacement
-
at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
-
diffraction to 2.4 A. Final model contains two tetramers displaying 222 symmetry and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates
-
structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism
-
purified recombinant enzyme, vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 6.8, 0.5 M NaCl, 1 mM DTT, and 0.5 mM EDTA, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.0, 35% v/v 2-methyl-2,4-pentanediol, and 0.2 M LiSO4, equilibration against 1 ml of mother liquor, room temperature, 6 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution
Q86RB1
purified native and selenomethionine-labeled recombinant enzyme, hanging drop vapour diffusion method, 18C, 2.5 mg/ml protein in 50 mm HEPES, pH 7.0, 5 mM Tris, pH 8.0, 0.15 mM ammonium sulfate, 6% PEG 4000, 0.1 M NaCl, 0.5 mM EDTA, and 0.5 mM DTT, mixed with reservoir solution containing 1 M HEPES, pH 7.0, 0.3 M ammonium sulfate, and 12% PEG 4000, plus 1 mM NADPH, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
crystalized at a resolution of 2.25 A
P50941, -
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
wild-type enzyme: about 15% loss of activity after 15 min, mutant enzyme E233K: about 60% loss of activity after 10 min,mutant enzyme A164T: about 20% loss of activity after 15 min, mutant enzyme A154T/E233K: about 80% loss of activity after 15 min
37
-
-
wild-type enzyme: about 40% loss of activity after 15 min, mutant enzyme E233K: about 90% loss of activity after 10 min, mutant enzyme A164T: about 25% loss of activity after 15 min, mutant enzyme A154T/E233K: about 80% loss of activity after 5 min
45
-
-
wild-type enzyme: about 70% loss of activity after 15 min, mutant enzyme E233K: complete loss of activity after 10 min, mutant enzyme A164T: about 60% loss of activity after 15 min, mutant enzyme A154T/E233K: complete loss of activity after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
inactivation by dilution can be partly prevented by inclusion of NADPH
-
inactivation by dilution can be partly prevented by inclusion of NADPH
-
the purified recombinant enzyme is stable at room temperature at concentrations above 0.2 mg/ml, but unstable at 0.01 mg/ml
Q86RB1
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
27C, 100 mM potassium phosphate buffer, 13% loss of activity after 24 h
-
4C, 100 mM potassium phosphate, 52% loss of activity after 24 h
-
-20C, phosphate buffer, 10% glycerol
-
-80C, 10% glycerol
P0AEK2
-80C, 50% glycerol
-
27C, 2 M NaCl, 24 h stable
-
-20C, stable for 2 months
-
-80C, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant protein
-
by nickel-affinity chromatography
-
by nickel affinity chromatography
-
by nickel chelation affinity chromatography
-
by sonication, centrifugation and on Ni-NTA column
P0AEK2
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant fatty acid synthase complex enzymes from Sf9 insect cells by nickel affinity chromatography, gel filtration, and dialysis
-
recombinant protein, modified purification protocol
-
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) solubilized from inclusion bodies and refolded is further purified by nickel affinity chromatography
-
recombinant His10-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
Q86RB1
wild-type and mutants purified to homogeneity using an Ni2+-nitrilotriacetic acid affinity column
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
Q4AE87
using Ni-NTA chromatography
P50941, -
by gel filtration and ion exchange chromatography, to homogeneity
Q31QF3
by nickel chelation affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
YFP-KCR1 and CFP-KCR2 fusion constructs transiently expressed in tobacco under the control of the 35S promoter or in Arabidopsis. KCR1 and KCR2 expressed in the yeast ybr159DELTA mutant
-
expression in Escherichia coli
-
PCR product recombined with pDONR221 and insert from this vector transferred in the LR reaction to the expression vector pET15g which adds a histidine tag and a 3C protease cleavage site, expressed in Escherichia coli B834(DE3) cells
-
expression in Escherichia coli
-
overexpression in Escherichia coli strain BL21 (DE3)
-
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter
Q949M3
expression in Saccharomyces cerevisae mutant cells lacking the homologous mitochondrial FASII enzyme 3-oxoacyl-ACP reductase Oar1p
-
expression of protein without transit peptide in Escherichia coli
-
coexpression in Escherichia coli LS5218 with fabH mutant F87T and polyhydroxyalkanoate synthase genes
-
gene fabG, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene fabG, overexpression of His-tagged enzyme in strain BL21(DE3)
-
His-tagged FabG expressed in Escherichia coli strain BL21 (DE3)
-
NH2-terminally His-tagged FabG expressed in Escherichia coli strain BL21(DE3)
-
overexpression of fabG gene in Escherichia coli strain BL21 (DE3)
-
pET15b-fabG vector construct transformed into the Escherichia coli BL21 DE3 strain
P0AEK2
heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with fabG1 in Haloferax volcanii
-
heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with Haloarcula hispanica fabG1 reconstructs the polyhydroxyalkanoate biosynthetic pathway
-
expression of His-tagged wild-type and mutant fatty acid synthase complex enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
-
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
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Streptomyces cerevisiae cells lacking 3-oxoacyl-ACP reductase; FabG1 expressed from vector pPLM189 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG1 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production; FabG4 expressed from vector pPLM192 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG4 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production
O53665, P0A5Y4
selection of an Escherichia coli, BL21(DE3)NH host that stably expresses mutant forms of 3-ketoacyl-ACP(CoA) reductase
-
expression in Escherichia coli
Q965D6
gene fabG, DNA and amino acid sequence determination and analysis, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene fabG, DNA and amino acid sequence determination and analysis, expression of His10-tagged enzyme in Escherichia coli
Q86RB1
into pET-28a vector and expressed in Escherichia coli BL21 (DE3) codon plus
-
overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
-
wild-type and mutants cloned into the pET-28a(+) vector and expressed in Escherichia coli BL21 (DE3) codon plus
-
gene rhlG, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) or, as selenomethionine-labeled variant in Escherichia coli strain B834 in minimal medium
-
Recombinant Escherichia coli (strain DH5alpha) co-expresses the fabG gene. The fabG gene is PCR-cloned using primers derived from the up and down-stream regions of the Pseudomonas putida KT2440 genome.
A5HIF6, -
gene fabG, overexpression of His-tagged enzyme in strain BL21(DE3), recombinant expression in Escherichia coli strain JM109 leads to enhanced production of polyhydroxyalkanoate, PHA, copolymer from glucose, PHA composition, overview
Q4AE87
expressed in Escherichia coli as a His-tagged fusion protein
P50941, -
transformation of the fabG gene encoding 3-ketoacyl-[acyl-carrier-protein] reductase in fusion with a His6-MBP-tag (ligated into vector pETM-41) into Escherichia coli XL-10 Gold. After isolation from XL-10 cells and DNA sequencing, transformed into Escherichia coli Tuner (DE3) cells
Q31QF3
overexpressed in Escherichia coli BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A154T
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similar thermal stability as wild-type enzyme
A154T/E233K
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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
E233K
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temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
F87T
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coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources
K1699A
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site-directed mutagenesis, the mutant BKR shows reduced Km for acetoacetyl-CoA, increased Km for NADPH and reduced activity compared to the wild-type enzyme
K1699Q
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site-directed mutagenesis, the mutant BKR shows reduced Km for acetoacetyl-CoA, increased Km for NADPH and reduced activity compared to the wild-type enzyme
S2151A
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site-directed mutagenesis, inactive mutant
S140A
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mutant shows no enzymatic activity. S140A mutant does not bind to NADPH
S140T
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mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding
R187A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 3fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187A/R230A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 4fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187E/R230E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. 80fold decreased affinity binding to acyl-carrier protein with respect to wild-type
R187K
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no decreased affinity binding to acyl-carrier protein with respect to wild-type
R230A
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 5fold decreased affinity binding to acyl-carrier protein with respect to wild-type
E233K
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42C in complementation assay
M125I/S233T
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42C in complementation assay
additional information
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insertional mutants in KCR1 and KCR2
additional information
Q949M3
transformation with 3-oxoacyl-[acyl-carrier-protein] reductase in antisense orientation, driven by either the cauliflower mosaic virus 35S promoter or a seed-specific acyl carrier protein promoter. In plants with altered reductase activity, total seed yield is reduced in all cases. In less severely affected plant lines, seeds have a normal appearance and composition but the yield of seeds is reduced by approximately 50%. In more severely affected lines, reductions in both seed fatty acid content and the number of seeds produced per plant are evident, resulting in a 90% reduction in fatty acid synthesized per plant. Phenotypes are independent of the promoter used. In severely affected lines, a large proportion of seeds show precocious germination, and these have a reduced oleate content and increased levels of polyunsaturated 18-carbon fatty acids, compared with normal seeds of the same line
additional information
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glutathione-S-transferase fusion protein without transit peptide, expressed in Escherichia coli
R230E
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kinetic constants (Km and acyl-carrier protein-independent specific activities) remain largely unchanged with respect to wild-type. Exhibits very poor activity in the acyl-carrier protein-dependent spectroscopic assay. No inhibition by increasing concentrations of acyl-carrier protein. 41fold decreased affinity binding to acyl-carrier protein with respect to wild-type
additional information
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mutant cells lacking the homologous mitochondrial FASII enzyme 3-oxoacyl-ACP reductase Oar1p
additional information
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oar1-DELTA mutants, lack 3-oxoacyl-ACP reductase acitivity, expression of FabG4 gene of Mycobacterium tuberculosis
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
solubilization of overexpressed recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) inclusion bodies by 8 M urea, and refolding by dialysis, cation exchange chromatography, and dilution in presence of 0.001 mM NADPH in 20 mM sodium acetate, pH 5.3, 10% glycerol, and 0.05% Tween 20, the refolded enzyme shows 90-95% of soluble enzyme activity
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study on guanidinium chloride-induced isothermal and thermal denaturation. Folding/unfolding is completely reversible and a two-state process. Conformational stability, i.e. DELTAGS, and the DELTACP value for the protein unfolding, are 22.68 kcal/mole and 5.83 kcal/(mole K)
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Acinetobacter calcoaceticus 25001
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Enterobacter aerogenes 45102
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Enterobacter cloacae 45301
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
synthesis
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coexpression with fabH mutant F87T and polyhydroxyalkanoate synthase genes enhances the production of short chain length-medium chain length polyhydroxyalkanoate copolymer from both related and unrelated carbon sources. Analysis of polyhydroxyalkanoate accumulation and physical characterization of copolymer
drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
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the enzyme has no isoforms and thus is a good target for inhibitor design
drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
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galangal extract inhibits FabG, thereby displaying antibacterial ability
drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Pseudomonas aeruginosa ATCC27853
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galangal extract inhibits FabG, thereby displaying antibacterial ability
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Salmonella enterica subsp. enterica serovar Typhi H901
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Serratia marcescens 41002
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Shigella sonnei 51592
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
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drug development
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galangal extract inhibits FabG, thereby displaying antibacterial ability
drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
Staphylococcus aureus ATCC25923
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galangal extract inhibits FabG, thereby displaying antibacterial ability
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drug development
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FabG is the antibacteria target of maple leaf extracts and tannic acid, and both reversible and irreversible inhibitions of FabG are important for the antibacterial effect
drug development
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galangal extract inhibits FabG, thereby displaying antibacterial ability