Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Homo sapiens

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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
1.1.1.100
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RECOMMENDED NAME
GeneOntology No.
3-oxoacyl-[acyl-carrier-protein] reductase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodecenoate biosynthesis I
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(5Z)-dodecenoate biosynthesis II
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8-amino-7-oxononanoate biosynthesis I
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cis-vaccenate biosynthesis
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fatty acid elongation -- saturated
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gondoate biosynthesis (anaerobic)
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mycolate biosynthesis
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
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oleate biosynthesis IV (anaerobic)
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palmitate biosynthesis I (animals and fungi)
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palmitate biosynthesis II (bacteria and plants)
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palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)
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petroselinate biosynthesis
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stearate biosynthesis II (bacteria and plants)
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stearate biosynthesis III (fungi)
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superpathway of mycolate biosynthesis
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arachidonate biosynthesis
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cis-vaccenate biosynthesis
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lipid metabolism
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palmitate biosynthesis
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Fatty acid biosynthesis
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Biotin metabolism
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Biosynthesis of unsaturated fatty acids
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Metabolic pathways
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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 hide
37250-34-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
9,10-phenanthrene quinone + NADH + H+
?
show the reaction diagram
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?
9,10-phenanthrene quinone + NADPH + H+
?
show the reaction diagram
low activity with NADPH
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?
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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?
acetoacetyl-CoA + NADH + H+
?
show the reaction diagram
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?
acetoacetyl-CoA + NADPH + H+
?
show the reaction diagram
low activity with NADPH
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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
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
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compound is transported across cancer cell membrane to further down-regulate FAS and activate caspase-3 in MDA-MB-231 cells. Compared with other FAS inhibitors, including catechin gallate and morin, 1,2,3,4,6-penta-O-galloyl-beta-D-glucose involves a higher reversible fast-binding inhibition with an irreversible slow-binding inhibition, i.e. saturation kinetics with a dissociation constant of 0.59 microM and a limiting rate constant of 0.16 per min. The major reacting site of PGG is on the beta-ketoacyl reduction domain of FAS. Compound exhibits different types of inhibitions against the three substrates in the FAS overall reaction
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
mutant enzyme K173A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
0.44
mutant enzyme R34A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C; mutant enzyme R34A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
0.46
mutant enzyme K152A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
0.5
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
0.65
mutant enzyme Y169A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
0.85
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
1.2
mutant enzyme K173A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
1.3
mutant enzyme K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
1.6
mutant enzyme R168E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
1.7
mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
2
mutant enzyme Y169A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
2.4
mutant enzyme K173A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
2.6
wild type enzyme, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
3.1
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
3.5
wild type enzyme, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
4.3
mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
4.5
mutant enzyme K173A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
5.4
mutant enzyme D42A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
5.5
mutant enzyme K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
6.3
mutant enzyme R168E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
7.3
mutant enzyme D42A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
7.9
mutant enzyme R168E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
8.4
mutant enzyme Q126E/R168E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
14.8
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
15.7
mutant enzyme K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
17.4
mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
19.3
mutant enzyme K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
20
mutant enzyme D42A, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
20.5
wild type enzyme, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
20.7
mutant enzyme R34A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
20.8
wild type enzyme, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
21
mutant enzyme R34A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
21.7
mutant enzyme R168E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
22
mutant enzyme K152A, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
25.5
mutant enzyme K152A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
31.8
mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
74.6
mutant enzyme D42A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 15-18% (w/v) PEG3350 and 0.4 M ammonium acetate in sodium acetate buffer at pH 5.0
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (RARE) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D42A
the mutant shows 36% activity with acetoacetyl-CoA and NADH, 20% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 26% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K152A
the mutant shows 109% activity with acetoacetyl-CoA and NADH, no activity with acetoacetyl-CoA and NADPH, 123% activity with 9,10-phenanthrene and NAD+, and 2.2% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K169E
the mutant shows 95% activity with acetoacetyl-CoA and NADH, 5.5% activity with acetoacetyl-CoA and NADPH, 76% activity with 9,10-phenanthrene and NAD+, and 6% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
K173A
the mutant shows 0.3% activity with acetoacetyl-CoA and NADH, 2.4% activity with acetoacetyl-CoA and NADPH, 6% activity with 9,10-phenanthrene and NAD+, and 22% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/K169E
the mutant shows 156% activity with acetoacetyl-CoA and NADH, 4.3% activity with acetoacetyl-CoA and NADPH, 84% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Q126E/R168E/K169E
the mutant shows 72% activity with acetoacetyl-CoA and NADH, 0.5% activity with acetoacetyl-CoA and NADPH, 40% activity with 9,10-phenanthrene and NAD+, and no activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R168E
the mutant shows 106% activity with acetoacetyl-CoA and NADH, 6.3% activity with acetoacetyl-CoA and NADPH, 38% activity with 9,10-phenanthrene and NAD+, and 8% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
R34A
the mutant shows 102% activity with acetoacetyl-CoA and NADH, 100% activity with acetoacetyl-CoA and NADPH, 40.44% activity with 9,10-phenanthrene and NAD+, and 2.1% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively
Y169A
the mutant shows 3% activity with acetoacetyl-CoA and NADH, 2% activity with acetoacetyl-CoA and NADPH, 4% activity with 9,10-phenanthrene and NAD+, and 15% activity with 9,10-phenanthrene and NADP+, compared to the wild type enzyme, respectively