1.1.1.330: very-long-chain 3-oxoacyl-CoA reductase
This is an abbreviated version!
For detailed information about very-long-chain 3-oxoacyl-CoA reductase, go to the full flat file.
Word Map on EC 1.1.1.330
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1.1.1.330
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elongase
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vlcfas
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protein-tagged
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sphingolipids
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dihydrosphingosine
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ceramides
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waxes
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cuticular
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phytosphingosine
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palmitoyl-coa
- 1.1.1.330
- elongase
-
vlcfas
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protein-tagged
- sphingolipids
- dihydrosphingosine
- ceramides
- waxes
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cuticular
- phytosphingosine
- palmitoyl-coa
Reaction
Synonyms
3-ketoacyl-CoA reductase, beta-ketoacyl-CoA reductase, EC 2.3.1.119, ECR, IFA38, KCR, KCR1, KCR2, KCR3, very-long-chain 3-ketoacyl-CoA reductase, very-long-chain beta-ketoacyl-CoA reductase, very-long-chain enoyl-CoA reductase, ybr159, YBR159w
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General Information
General Information on EC 1.1.1.330 - very-long-chain 3-oxoacyl-CoA reductase
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physiological function
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
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 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
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
physiological function
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the enzyme affects rice cuticular wax production by participating in very long-chain fatty acid elongation