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Enzyme Nomenclature
Information on EC 1.1.1.330 - very-long-chain 3-oxoacyl-CoA reductase
Word Map on EC 1.1.1.330
- 1.1.1.330
- elongase
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vlcfas
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candida
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short-chain
- steroid
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sphingolipids
- dihydrosphingosine
- phytosphingosine
- reticulum
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dehydration
- palmitoyl-coa
- ceramides
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protein-tagged
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.330
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RECOMMENDED NAME
GeneOntology No.
very-long-chain 3-oxoacyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH + H+
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9028-40-4
cf. EC 1.1.1.35
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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expression of isoform KCR1 can restore heterologous elongase activity in yeast. Loss of isoform KCR1 function results in embryo lethality, while loss loss of isoform KCR2 function has no obvious phenotypic effect. Suppression of isoform KCR1 enzymic activity results in a reduction of cuticular wax load and affects very-long-chain fatty acid composition of sphingolipids, seed triacylglycerols, and root glycerolipids
physiological function
gene is able to complement the yeast ybr159w deletion mutant. Yeast ybr159w deletion mutant cells expressing the gene produce very long-chain fatty acids, especially C26:0. Enzyme does not participate in plastid de novo fatty acid synthesis pathway but is possibly involved in a cytosolic fatty acid elongation system
physiological function
heterologous expression in a yeast ybr159w deletion mutant restores wild-type grwoth; heterologous expression in a yeast ybr159w deletion mutant restores wild-type grwoth
physiological function
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gene disruption results in slow growth of mutants and high temperature sensitivity. Enzyme is a component of the microsomal fatty acid elongase complex, mutants display reduced endogenous fatty acid elongation activity
physiological function
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a Ybr159 gene disruption mutant shows reduced very long-chain fatty acid synthesis, accumulation of high levels of dihydrosphingosine and phytosphingosine, and accumulation of medium-chain ceramides. Mutant is deficient in the reduction of the 3-ketoacyl intermediates of fatty acid elongation. The mutant also displays reduced dehydration of the 3-OH acyl intermediates of fatty acid elongation, suggesting that its gene is required for the stability or function of the dehydratase activity of the elongase system. The enzyme protein co-localizes and co-immunoprecipitates with other elongating enzymes, Elo3p and Tsc13p. Whereas very long-chain fatty acid synthesis is essential for viability, the deletion mutant cells are viable albeit very slowly growing and do synthesize some very long-chain fatty acids. A ybr159ayr1 double mutant is inviable, suggesting that Ayr1p is responsible for the residual 3-ketoreductase activity
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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
(3R)-3-hydroxy-lignoceroyl-CoA + NADP+
3-oxo-lignoceroyl-CoA + NADPH + H+
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?
3-oxostearoyl-CoA + NADPH + H+
3-hydroxystearoyl-CoA + NADP+
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additional information
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enzyme shows NADPH-dependent 3-ketoacyl-CoA reductase activity in an in vitro fatty acid elongation assay system using palmitoyl-CoA and malonyl-CoA as substrates
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additional information
?
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enzyme shows NADPH-dependent 3-ketoacyl-CoA reductase activity in an in vitro fatty acid elongation assay system using palmitoyl-CoA and malonyl-CoA as substrates
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
developing fiber, high expression during the cotton fiber elongation period; developing fiber, high expression during the cotton fiber elongation period
additional information
gene KCR3 transcripts accumulate in rapidly elongating fibers, roots and stem
gene KCR3 transcripts accumulate in rapidly elongating fibers, roots and stem
additional information
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gene KCR3 transcripts accumulate in rapidly elongating fibers, roots and stem. Expression is found in all of the cotton tissues tested, including ovules, roots, leaves, and flowers
additional information
gene KCR3 transcripts accumulate in rapidly elongating fibers, roots and stem. Expression is found in all of the cotton tissues tested, including ovules, roots, leaves, and flowers
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.330)
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