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

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

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EC NUMBER
COMMENTARY hide
1.1.1.100
-
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RECOMMENDED NAME
GeneOntology No.
3-oxoacyl-[acyl-carrier-protein] reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodec-5-enoate biosynthesis
-
-
8-amino-7-oxononanoate biosynthesis I
-
-
arachidonate biosynthesis
-
-
Biosynthesis of unsaturated fatty acids
-
-
Biotin metabolism
-
-
cis-vaccenate biosynthesis
Fatty acid biosynthesis
-
-
fatty acid elongation -- saturated
-
-
gondoate biosynthesis (anaerobic)
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
mycolate biosynthesis
-
-
octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
-
-
oleate biosynthesis IV (anaerobic)
-
-
palmitate biosynthesis
-
-
palmitate biosynthesis I (animals and fungi)
-
-
palmitate biosynthesis II (bacteria and plants)
-
-
palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)
-
-
petroselinate biosynthesis
-
-
stearate biosynthesis II (bacteria and plants)
-
-
stearate biosynthesis III (fungi)
-
-
superpathway of mycolate biosynthesis
-
-
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SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-34-3
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 25001
-
-
Manually annotated by BRENDA team
strain 25001
-
-
Manually annotated by BRENDA team
isoform FabG
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
rapeseed
-
-
Manually annotated by BRENDA team
safflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 45102
-
-
Manually annotated by BRENDA team
strain 45102
-
-
Manually annotated by BRENDA team
strain 45301
-
-
Manually annotated by BRENDA team
strain 45301
-
-
Manually annotated by BRENDA team
strains ATCC29212 and 775
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain AS2049
-
-
Manually annotated by BRENDA team
strain AS2049
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strains ATCC700603 and 14
-
-
Manually annotated by BRENDA team
ssp. lactis IL 1403
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ATCC27853
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain 61-3, non-pathogenic strain from soil, gene fabG
SwissProt
Manually annotated by BRENDA team
strain 41002
-
-
Manually annotated by BRENDA team
strain 41002
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 51592
-
-
Manually annotated by BRENDA team
strain 51592
-
-
Manually annotated by BRENDA team
ATCC25923
-
-
Manually annotated by BRENDA team
alpha-haemolytic strain 32213-7 and beta-haemolytic strain 32210-20
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
beta-oxidation pathway
-
-
?
1,1,1-trifluoroacetone + NADPH
? + NADP+
show the reaction diagram
792% relative activity compared to acetophenone
-
-
?
2',3',4',5',6'-pentafluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
3023% relative activity compared to acetophenone
-
-
?
2-octanone + NADPH
? + NADP+
show the reaction diagram
15% relative activity compared to acetophenone
-
-
?
3'-fluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
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
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
3-oxodecanoyl-CoA + NADPH
(R)-3-hydroxydecanoyl-CoA + NADP+
show the reaction diagram
3-oxododecanoyl-CoA + NADPH
(R)-3-hydroxydodecanoyl-CoA + NADP+
show the reaction diagram
3-oxohexanoyl-CoA + NADPH
(R)-3-hydroxyhexanoyl-CoA + NADP+
show the reaction diagram
3-oxooctanoyl-CoA + NADPH
(R)-3-hydroxyoctanoyl-CoA + NADP+
show the reaction diagram
4'-chloroacetophenone + NADPH
? + NADP+
show the reaction diagram
115% relative activity compared to acetophenone
-
-
?
4'-fluoroacetophenone + NADPH
? + NADP+
show the reaction diagram
62% relative activity compared to acetophenone
-
-
?
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-CoA + NADPH
D-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + NADPH
D-beta-hydroxybutyryl-CoA + 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
acetophenone + NADPH
? + NADP+
show the reaction diagram
100% relative activity
-
-
?
alpha-chloroacetophenone + NADPH
? + NADP+
show the reaction diagram
1885% relative activity compared to acetophenone
-
-
?
beta-ketoacyl-[acyl-carrier protein] + NADPH
beta-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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
-
-
-
ethyl 4-chloroacetoacetate + NADPH
? + NADP+
show the reaction diagram
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
ethylbenzoylacetate + NADPH
? + NADP+
show the reaction diagram
892% relative activity compared to acetophenone
-
-
?
methyl acetoacetate + NADPH
? + NADP+
show the reaction diagram
-
is not a good substrate as ethyl acetoacetate
-
-
?
propiophenone + NADPH
? + NADP+
show the reaction diagram
123% relative activity compared to acetophenone
-
-
?
propyl acetoacetate + NADPH
? + NADP+
show the reaction diagram
-
as substrate it is limited to its weak solubility
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(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
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
NADPH is much more effective than NADH
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme activity is maximal at a ionic strength of 325 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-1-(4-methylpiperidin-1-yl)-3-phenylprop-2-en-1-one
80% residual activity
(E)-2-nitrophenyl cinnamate
-
(E)-3-phenoxybenzyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
61% residual activity
(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
-
(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
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
3-hydroxybutyryl-CoA
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
over 75% inhibition at 0.02 mM, IC50: 0.010 mM
bromochlorophen
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
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
an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM
kaempferol
synthetic construct
-
-
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
69% residual activity
p-chloromercuribenzoate
-
-
Phenylglyoxal
quercetin
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
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
89.2
1,1,1-trifluoroacetone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
5.72
2',3',4',5',6'-pentafluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
7.38
3'-fluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
14.34
4'-chloroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
12.29
4'-fluoroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.075 - 2.2
acetoacetyl-CoA
48
acetoacetyl-N-acetylcysteamine
-
-
0.003 - 0.017
acetoacetyl-[acyl-carrier protein]
46.92
acetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2.71
alpha-chloroacetophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.29 - 4.06
beta-ketobutyryl-CoA
8.31
ethyl 4-chloroacetoacetate
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.127
ethyl acetoacetate
-
-
1.92
ethylbenzoylacetate
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.035
N-acetoacetyl-N-cysteamine
-
-
-
0.0093 - 0.4553
NADPH
6.03
propiophenone
with 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 265
acetoacetyl-CoA
0.3
ethyl acetoacetate
Escherichia coli
-
-
0.59 - 344.7
NADPH
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0102
3-hydroxybutyryl-CoA
pH 6.8, 25°C, recombinant enzyme
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
(E)-2-nitrophenyl cinnamate
Escherichia coli
P0AEK2
pH 7.0
0.18
(E)-4-cyanophenyl 3-(benzo[d][1,3]dioxol-5-yl)acrylate
0.5
4-acetoxyanthecotulide
Plasmodium falciparum K1
-
pH 7.0, 25°C
0.75
4-hydroxyanthecotulide
Plasmodium falciparum K1
-
pH 7.0, 25°C
1
anthecotulide
Plasmodium falciparum K1
-
pH 7.0, 25°C
0.01
Bithionol
Plasmodium falciparum
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.010 mM
0.0154
bromochlorophen
Plasmodium falciparum
Q86RB1
an anthelmintic agent, over 75% inhibition at 0.02 mM, IC50: 0.0154 mM
0.881 - 0.948
chlorogenic acid
Escherichia coli
-
IC50: 0.881-0.948 mM
0.0038
di-resorcinol sulfide
Plasmodium falciparum
Q86RB1
over 75% inhibition at 0.02 mM, IC50: 0.0038 mM
0.00554 - 0.1223
epigallocatechin gallate
0.002
Hexachlorophene
Plasmodium falciparum
Q86RB1
an anthelmintic and antimicrobial agent, over 75% inhibition at 0.02 mM, IC50: 0.002 mM
0.0212
kaempferol
synthetic construct
-
pH 7.0
0.215
N-(1,3-dioxoisoindolin-2-yl)-2-oxo-2H-chromene-3-carboxamide
Escherichia coli
P0AEK2
pH 7.0
0.3048
quercetin
synthetic construct
-
pH 7.0
0.00078
Tannic acid
Escherichia coli
-
-
additional information
additional information
synthetic construct
-
IC(50) value of 4.47 microg/ml for extract of galangal, pH 7.0
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0017 - 0.0018
-
recombinant refolded enzyme
0.0019
-
recombinant soluble enzyme
0.0132
-
-
0.0168
-
-
0.02
with 2-octanone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.0366
-
-
0.08
with 4'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.13
with 3'-fluoroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0; with acetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.15
with 4'-chloroacetophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
0.16
with propiophenone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.03
with 1,1,1-trifluoroacetone as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
1.16
with ethylbenzoylacetate as substrate, 4 mM NADPH, in 0.1 M sodium phosphate buffer, pH 7.0
2
-
mutant R187E/R230E, acyl-carrier protein-dependent spectroscopic assay
2.45
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
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
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
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 6.2
-
-
7.5
-
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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 37
-
temperature profile
30 - 55
30°C: about 55% of maximal activity, 55°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
strain KCTC1639
Manually annotated by BRENDA team
-
KCR1 and KCR2
Manually annotated by BRENDA team
-
KCR1 and KCR2 present in inflorescence stem
Manually annotated by BRENDA team
-
KCR1 and KCR2
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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 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)
Burkholderia xenovorans (strain LB400)
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 tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
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)
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)
Staphylococcus aureus (strain NCTC 8325)
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 ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25500
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
110000
-
gel filtration, wild-type and mutants
116000
-
recombinant enzyme, analytical ultracentrifugation, tetrameric at higher enzyme concentrations
120000
-
gel filtration
130000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 29000, recombinant enzyme, SDS-PAGE
homotetramer
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4 * 31000, SDS-PAGE, wild-type and mutants
tetramer
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme contains a signal peptide
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.8 A, determinantion of initial phases by molecular replacement
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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
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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
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structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism
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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
purified native and selenomethionine-labeled recombinant enzyme, hanging drop vapour diffusion method, 18°C, 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
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crystalized at a resolution of 2.25 A
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, phosphate buffer, 10% glycerol
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-20°C, stable for 2 months
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-80°C, 10% glycerol
-80°C, 50% glycerol
27°C, 100 mM potassium phosphate buffer, 13% loss of activity after 24 h
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27°C, 2 M NaCl, 24 h stable
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4°C, 100 mM potassium phosphate, 52% loss of activity after 24 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by gel filtration and ion exchange chromatography, to homogeneity
by nickel affinity chromatography
-
by nickel chelation affinity chromatography
by nickel-affinity chromatography
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by sonication, centrifugation and on Ni-NTA column
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) solubilized from inclusion bodies and refolded is further purified by nickel affinity chromatography
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recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
recombinant His10-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant protein
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recombinant protein, modified purification protocol
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using Ni-NTA chromatography
wild-type and mutants purified to homogeneity using an Ni2+-nitrilotriacetic acid affinity column
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression in Escherichia coli LS5218 with fabH mutant F87T and polyhydroxyalkanoate synthase genes
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complementation of Escherichia coli fabG mutant with Lactobacillus lactis fabG genes shows that fabG1 encodes a functional beta-ketoacyl ACP reductase and fabG2 encodes an enzyme that has activity with the model substrate beta-ketobutyryl-CoA, but lacks the ability to support fatty acid synthesis both in vivo and in vitro
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expressed in Escherichia coli
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expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
expression in Saccharomyces cerevisae mutant cells lacking the homologous mitochondrial FASII enzyme 3-oxoacyl-ACP reductase Oar1p
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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
expression of protein without transit peptide in Escherichia coli
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gene fabG, DNA and amino acid sequence determination and analysis, expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene fabG, DNA and amino acid sequence determination and analysis, expression of His10-tagged enzyme in Escherichia coli
gene fabG, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
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gene fabG, overexpression of His-tagged enzyme in strain BL21(DE3)
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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
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
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heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with fabG1 in Haloferax volcanii
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heterologous coexpression of the polyhydroxyalkanoate synthase genes phaEC together with Haloarcula hispanica fabG1 reconstructs the polyhydroxyalkanoate biosynthetic pathway
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His-tagged FabG expressed in Escherichia coli strain BL21 (DE3)
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into pET-28a vector and expressed in Escherichia coli BL21 (DE3) codon plus
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NH2-terminally His-tagged FabG expressed in Escherichia coli strain BL21(DE3)
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overexpressed in Escherichia coli BL21 (DE3)
synthetic construct
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overexpression in Escherichia coli strain BL21 (DE3)
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overexpression of fabG gene in Escherichia coli strain BL21 (DE3)
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overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
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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
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pET15b-fabG vector construct transformed into the Escherichia coli BL21 DE3 strain
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.
selection of an Escherichia coli, BL21(DE3)NH host that stably expresses mutant forms of 3-ketoacyl-ACP(CoA) reductase
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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
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
wild-type and mutants cloned into the pET-28a(+) vector and expressed in Escherichia coli BL21 (DE3) codon plus
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A154T
-
similar thermal stability as wild-type enzyme
A154T/E233K
-
temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
E233K
-
temperature-sensitive phenoptype, reductase activity is much more thermolabile than the activity of the wild-type strain
F87T
-
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
S140A
-
mutant shows no enzymatic activity. S140A mutant does not bind to NADPH
S140T
-
mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding
R187A
-
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
-
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
-
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
-
no decreased affinity binding to acyl-carrier protein with respect to wild-type
R230A
-
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
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
E233K
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
M125I/S233T
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temperature-sensitive mutant enzyme does not allow growth of Escherichia coli at 42°C in complementation assay
additional information
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Renatured/COMMENTARY
ORGANISM
UNIPROT
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
COMMENTARY hide
LITERATURE
drug development
synthesis
-
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
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Show AA Sequence (17824 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.100)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)