Information on EC 1.1.1.330 - very-long-chain 3-oxoacyl-CoA reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.330
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RECOMMENDED NAME
GeneOntology No.
very-long-chain 3-oxoacyl-CoA reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis (6-desaturase)
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(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis II (4-desaturase)
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arachidonate biosynthesis I (6-desaturase, lower eukaryotes)
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arachidonate biosynthesis III (6-desaturase, mammals)
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arachidonate biosynthesis IV (8-detaturase, lower eukaryotes)
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arachidonate biosynthesis V (8-detaturase, mammals)
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Biosynthesis of secondary metabolites
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Biosynthesis of unsaturated fatty acids
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docosahexaenoate biosynthesis I (lower eukaryotes)
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docosahexaenoate biosynthesis III (6-desaturase, mammals)
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docosahexaenoate biosynthesis IV (4-desaturase, mammals)
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Fatty acid elongation
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hydroxylated fatty acid biosynthesis (plants)
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icosapentaenoate biosynthesis I (lower eukaryotes)
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icosapentaenoate biosynthesis II (6-desaturase, mammals)
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icosapentaenoate biosynthesis III (8-desaturase, mammals)
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icosapentaenoate biosynthesis V (8-desaturase, lower eukaryotes)
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juniperonate biosynthesis
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sciadonate biosynthesis
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very long chain fatty acid biosynthesis I
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very long chain fatty acid biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase
The second component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long-chain acyl CoAs. The enzyme is active with substrates with chain length of C16 to C34, depending on the species. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-40-4
cf. EC 1.1.1.35
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-hydroxy-arachidoyl-CoA + NADP+
3-oxo-arachidoyl-CoA + NADPH + H+
show the reaction diagram
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?
(3R)-3-hydroxy-lignoceroyl-CoA + NADP+
3-oxo-lignoceroyl-CoA + NADPH + H+
show the reaction diagram
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?
3-oxostearoyl-CoA + NADPH + H+
3-hydroxystearoyl-CoA + NADP+
show the reaction diagram
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?
nonanal + NADPH + H+
1-nonanol + NADP+
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
NADPH
pH 7.5, 37°C
0.026
Nonanal
pH 7.5, 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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developing embryo
Manually annotated by BRENDA team
developing fiber, high expression during the cotton fiber elongation period; developing fiber, high expression during the cotton fiber elongation period
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34500
x * 34500, calculated and SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34500, calculated and SDS-PAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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