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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Homo sapiens and UniProt Accession Q92506
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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: Homo sapiens
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
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3-oxoacyl-[ACP]reductase
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beta-ketoacyl acyl carrier protein (ACP) reductase
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beta-ketoacyl reductase
beta-ketoacyl thioester reductase
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beta-ketoacyl-ACP reductase
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beta-ketoacyl-acyl carrier protein reductase
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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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beta-ketoacyl 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
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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-
-
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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
a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
0.44
0.46
mutant enzyme K152A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
0.5
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADPH, pH 7.4 and 25°C
0.85
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
1.2
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
14.8
mutant enzyme Q126E/R168E/K169E, with acetoacetyl-CoA and NADH, pH 7.4 and 25°C
15.7
mutant enzyme K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
17.4
mutant enzyme Q126E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
2.6
wild type enzyme, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
20.7
mutant enzyme R34A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
20.8
wild type enzyme, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
25.5
mutant enzyme K152A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
3.1
mutant enzyme Y169A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
31.8
mutant enzyme Q126E/K169E, with acetoacetyl-CoA and NADH, 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
7.9
mutant enzyme R168E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
74.6
mutant enzyme D42A, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
8.4
mutant enzyme Q126E/R168E/K169E, with 9,10-phenanthrene quinone and NAD+, pH 7.4 and 25°C
0.44
mutant enzyme R34A, with 9,10-phenanthrene quinone and NADP+, pH 7.4 and 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhao, W.; Wang, Y.; Hao, W.; Zhao, M.; Peng, S.
In vitro inhibition of fatty acid synthase by 1,2,3,4,6-penta-O-galloyl-beta-D-glucose plays a vital role in anti-tumour activity
Biochem. Biophys. Res. Commun.
445
346-351
2014
Homo sapiens
Venkatesan, R.; Sah-Teli, S.K.; Awoniyi, L.O.; Jiang, G.; Prus, P.; Kastaniotis, A.J.; Hiltunen, J.K.; Wierenga, R.K.; Chen, Z.
Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase
Nat. Commun.
5
4805
2014
Homo sapiens (Q92506), Homo sapiens
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