Very-long-chain 3-oxoacyl-CoA reductase

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Very-long-chain 3-oxoacyl-CoA reductase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Very-long-chain 3-oxoacyl-CoA reductase (EC, very-long-chain 3-ketoacyl-CoA reductase, very-long-chain beta-ketoacyl-CoA reductase, KCR (gene), IFA38 (gene)) is an enzyme with systematic name (3R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction

a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ a very-long-chain 3-oxoacyl-CoA + NADPH + H+

This microsomal complex extendins palmitoyl-CoA and stearoyl-CoA (and their modified forms) to very-long-chain acyl CoAs.


  1. ^ Beaudoin, F.; Gable, K.; Sayanova, O.; Dunn, T.; Napier, J.A. (2002). "A Saccharomyces cerevisiae gene required for heterologous fatty acid elongase activity encodes a microsomal β-keto-reductase". J. Biol. Chem. 277 (13): 11481–11488. doi:10.1074/jbc.M111441200. PMID 11792704. 
  2. ^ Han, G.; Gable, K.; Kohlwein, S.D.; Beaudoin, F.; Napier, J.A.; Dunn, T.M. (2002). "The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase". J. Biol. Chem. 277 (38): 35440–35449. doi:10.1074/jbc.M205620200. PMID 12087109. 
  3. ^ Beaudoin, F.; Wu, X.; Li, F.; Haslam, R.P.; Markham, J.E.; Zheng, H.; Napier, J.A.; Kunst, L. (2009). "Functional characterization of the Arabidopsis β-ketoacyl-coenzyme A reductase candidates of the fatty acid elongase". Plant Physiol. 150 (3): 1174–1191. doi:10.1104/pp.109.137497. PMC 2705042Freely accessible. PMID 19439572. 

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