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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Escherichia coli and UniProt Accession P0AEK2
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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
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enoyl
- drug development
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transacylase
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3-oxoacyl-acyl-carrier-protein
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dehydrase
- enoyl-acp
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3-oxoacyl-acyl
- acyl-acps
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beta-hydroxyacyl-acp
- fas-ii
- 4'-phosphopantetheine
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
beta-ketoacyl reductase, fabg1, beta-ketoacyl-acp reductase, fabg4, 3-oxoacyl-acp reductase, fabg3, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-acp reductase, fabg2, oar1p, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl acyl carrier protein reductase
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3-ketoacyl-acyl carrier protein reductase
3-oxoacyl-[ACP]reductase
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beta-ketoacyl acyl carrier protein (ACP) reductase
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beta-ketoacyl reductase
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beta-ketoacyl thioester reductase
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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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NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
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reductase, 3-oxoacyl-[acyl carrier protein]
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3-ketoacyl-acyl carrier protein reductase
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beta-ketoacyl-ACP reductase
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beta-ketoacyl-acyl carrier protein reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
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-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
acetoacetyl-N-cysteamine + NADPH
D-3-hydroxybutyryl-N-cysteamine + NADP+
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-
-
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?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
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first reductive step in the elongation cycle of fatty acid biosynthesis
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?
methyl acetoacetate + NADPH
? + NADP+
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is not a good substrate as ethyl acetoacetate
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?
propyl acetoacetate + NADPH
? + NADP+
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as substrate it is limited to its weak solubility
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?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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r
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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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+
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first reduction step of fatty acid synthase
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?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
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?
acetoacetyl-CoA + NADPH + H+
D-beta-hydroxybutyryl-CoA + NADP+
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r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
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?
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
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r
acetoacetyl-[acyl-carrier protein] + NADPH
D-beta-hydroxybutyryl-[acyl-carrier protein] + NADP+
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r
additional information
?
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beta-ketoacyl thioesters of CoA and pantetheine metabolized at slower rates
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?
additional information
?
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equally active on beta-ketoacyl-ACP derivatives of C4 to C16
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?
additional information
?
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broad specificity for chain length of substrates
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?
additional information
?
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broad specificity for chain length of substrates
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?
additional information
?
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catalyzes also the reduction of the beta-keto group of unsaturated acyl chains during biosynthesis of unsaturated fatty acids
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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
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
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first reductive step in the elongation cycle of fatty acid biosynthesis
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?
additional information
?
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catalyzes also the reduction of the beta-keto group of unsaturated acyl chains during biosynthesis of unsaturated fatty acids
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?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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?
3-oxoacyl-[acyl-carrier protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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first reduction step of fatty acid synthase
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
69% residual activity
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
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mixed type of inhibition. IC50 value 0.9 microgramm per ml, Ki value 0.21 microgramm per ml
Tannic acid
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strongest inhibition on FabG, shows time-dependent irreversible inhibition
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
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additional information
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cinnamic acid derivatives can be accommodated in the substrate-binding region of the active site, above the nicotinamide moiety of the NADPH cofactor
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additional information
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inhibition by leaf extracts from Acer platanoides, Acer campestre, Acer rubrum, Acer saccharum and Acer truncatum Bunge
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additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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inhibition kinetic analysis
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.215
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
Escherichia coli
pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the unsaturated fatty acid biosynthetic pathway
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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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
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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
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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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
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recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal His-tagged FabG from Escherichia coli is cloned into the NcoI and XhoI cloning sites of the vector pET28a, expressed in BL21 DE3 Escherichia coli
pET15b-fabG vector construct transformed into the Escherichia coli BL21 DE3 strain
coexpression in Escherichia coli LS5218 with fabH mutant F87T and polyhydroxyalkanoate synthase genes
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gene fabG, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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NH2-terminally His-tagged FabG expressed in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimakata, T.; Stumpf, P.K.
Purification and characterizations of beta-ketoacyl-[acyl-carrier-protein] reductase, beta-hydroxyacyl-[acylcarrier-protein] dehydrase, and enoyl-[acyl-carrier-protein] reductase from Spinacia oleracea leaves
Arch. Biochem. Biophys.
218
77-91
1982
Escherichia coli, Spinacia oleracea
Volpe, J.J.; Vagelos, P.R.
Saturated fatty acid biosynthesis and its regulation
Annu. Rev. Biochem.
42
21-60
1973
Escherichia coli
Toomey, R.E.; Wakil, S.J.
Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli
Biochim. Biophys. Acta
116
189-197
1966
Escherichia coli
Rafferty, J.B.; Fisher, M.; Langridge, S.J.; Martindale, W.; Thomas, N.C.; Simon, J.W.; Bithell, S.; Slabas, A.R.; Rice, D.W.
Crystallization of the NADP-dependent beta-keto acyl carrier protein reductase from Escherichia coli
Acta Crystallogr. Sect. D
54
427-429
1998
Escherichia coli
Fisher, M.; Kroon, J.T.M.; Martindale, W.; Stuitje, A.R.; Slabas, A.R.; Rafferty, J.B.
The x-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis
Structure
8
339-347
2000
Brassica napus, Escherichia coli
Lai, C.Y.; Cronan, J.E.
Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar typhimurium
J. Bacteriol.
186
1869-1878
2004
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Nomura, C.T.; Taguchi, K.; Gan, Z.; Kuwabara, K.; Tanaka, T.; Takase, K.; Doi, Y.
Expression of 3-ketoacyl-acyl carrier protein reductase (fabG) genes enhances production of polyhydroxyalkanoate copolymer from glucose in recombinant Escherichia coli JM109
Appl. Environ. Microbiol.
71
4297-4306
2005
Escherichia coli, Pseudomonas sp. (Q4AE87), Pseudomonas sp.
Li, B.H.; Ma, X.F.; Wu, X.D.; Tian, W.X.
Inhibitory activity of chlorogenic acid on enzymes involved in the fatty acid synthesis in animals and bacteria
IUBMB Life
58
39-46
2006
Escherichia coli
Zhang, F.; Luo, S.Y.; Ye, Y.B.; Zhao, W.H.; Sun, X.G.; Wang, Z.Q.; Li, R.; Sun, Y.H.; Tian, W.X.; Zhang, Y.X.
The antibacterial efficacy of aceraceous plant may be related to inhibition of bacterial beta-ketoacyl-ACP reductase (FabG)
Biotechnol. Appl. Biochem.
51
73-78
2008
Escherichia coli, Pseudomonas aeruginosa, Staphylococcus epidermidis
Nomura, C.T.; Tanaka, T.; Eguen, T.E.; Appah, A.S.; Matsumoto, K.; Taguchi, S.; Ortiz, C.L.; Doi, Y.
FabG mediates polyhydroxyalkanoate production from both related and nonrelated carbon sources in recombinant Escherichia coli LS5218
Biotechnol. Prog.
24
342-351
2008
Escherichia coli
Kristan, K.; Bratkovic, T.; Sova, M.; Gobec, S.; Prezelj, A.; Urleb, U.
Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli
Chem. Biol. Interact.
178
310-316
2009
Escherichia coli (P0AEK2), Escherichia coli
Sun, Y.H.; Cheng, Q.; Tian, W.X.; Wu, X.D.
A substitutive substrate for measurements of beta-ketoacyl reductases in two fatty acid synthase systems
J. Biochem. Biophys. Methods
70
850-856
2008
Escherichia coli
Wu, D.; Wu, X.D.; You, X.F.; Ma, X.F.; Tian, W.X.
Inhibitory effects on bacterial growth and b-ketoacyl-ACP reductase by different species of maple leaf extracts and tannic acid
Phytother. Res.
24
535-541
2009
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus 25001, Enterobacter cloacae, Enterobacter cloacae 45301, Enterococcus sp., Escherichia coli, Klebsiella aerogenes, Klebsiella aerogenes 45102, Klebsiella pneumoniae, Proteus vulgaris, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhi, Salmonella enterica subsp. enterica serovar Typhi H901, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Serratia marcescens 41002, Shigella dysenteriae, Shigella flexneri, Shigella sonnei, Shigella sonnei 51592, Staphylococcus aureus, Staphylococcus epidermidis
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Liu, C.; Qi, J.; Shan, B.; Ma, Y.
Tachyplesin causes membrane instability that kills multidrug-resistant bacteria by inhibiting the 3-ketoacyl carrier protein reductase FabG
Front. Microbiol.
9
825
2018
Acinetobacter baumannii, Klebsiella pneumoniae, Escherichia coli (P0AEK2), Staphylococcus aureus (Q2FZ53), Staphylococcus aureus NCTC 8325 (Q2FZ53), Klebsiella pneumoniae 5, Escherichia coli K12 (P0AEK2), Acinetobacter baumannii 1408
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