Information on EC 1.3.1.93 - very-long-chain enoyl-CoA reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.93
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RECOMMENDED NAME
GeneOntology No.
very-long-chain enoyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a very-long-chain acyl-CoA + NADP+ = a very-long-chain trans-2,3-dehydroacyl-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 II (4-desaturase)
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(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate biosynthesis (6-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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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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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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Fatty acid elongation
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Biosynthesis of unsaturated fatty acids
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
very-long-chain acyl-CoA:NADP+ oxidoreductase
This is the fourth 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. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase.
CAS REGISTRY NUMBER
COMMENTARY hide
69403-06-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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homology modeling of Tsc13 based on the structure of a trans-2-enoyl reductase from Homo sapiens, PDB ID 1YXM
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H
a very-long-chain acyl-CoA + NADP+
show the reaction diagram
trans-2-hexadecenoyl-CoA + NADPH + H
palmitoyl-CoA + NADP+
show the reaction diagram
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 very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H
a very-long-chain acyl-CoA + NADP+
show the reaction diagram
trans-2-hexadecenoyl-CoA + NADPH + H
palmitoyl-CoA + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
predominantly expressed in the fibres and young leaves
Manually annotated by BRENDA team
low expression in root, stem, mature leaves, and flowers
Manually annotated by BRENDA team
predominantly expressed in the fibres and young leaves, low expression in root, stem, mature leaves, and flowers
Manually annotated by BRENDA team
low expression in root, stem, mature leaves, and flowers
Manually annotated by BRENDA team
low expression in root, stem, mature leaves, and flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene TECR, cloning from liver cDNA, Ectopic expression of human trans-2-enoyl-CoA reductase TER in Saccharomyces cerevisiae TER homologue Tsc13-lowered cells
gene TSC13, recombinant expression as N-terminal FLAG3-tagged enzyme from pAKNF313 and pAKNF315, or as N-terminal HA2-tagged enzyme
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gene TSC13, TSC13 SSM library screening
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is about 9fold upregulated during cotton fibre elongation; expression is upregulated during cotton fibre elongation
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G225A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
G234A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
I231A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
P232A
mutant is not able to complement the growth defect of a yeast tsc13 mutant
D77A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E144A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E259A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
E91A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H137A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
H149A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
K140A
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mutant is not able to complement an enzyme deletion mutant. Mutant protein is present at wild-type levels and does not show altered membrane topology
K76A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
R141A
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mutant is not able to complement an enzyme deletion mutant. Mutant protein is present at wild-type levels and does not show altered membrane topology
Y103A
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mutation is not critical for function, mutant is able to complement an enzyme deletion mutant
Y138A
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mutant is not able to complement an enzyme deletion mutant, protein is unstable
additional information