ExplorEnz: EC 1.3.1.93

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1.3.1.93

Accepted name:

very-long-chain enoyl-CoA reductase

Reaction:

a very-long-chain acyl-CoA + NADP⁺ = a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H⁺

Glossary:

a very-long-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains 23 or more carbon atoms.

Other name(s):

TSC13 (gene name); CER10 (gene name)

Systematic name:

very-long-chain acyl-CoA:NADP⁺ oxidoreductase

Comments:

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-CoA dehydratase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Kohlwein, S.D., Eder, S., Oh, C.S., Martin, C.E., Gable, K., Bacikova, D. and Dunn, T. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell Biol. 21 (2001) 109–125. [DOI] [PMID: 11113186]
2.	Gable, K., Garton, S., Napier, J.A. and Dunn, T.M. Functional characterization of the Arabidopsis thaliana orthologue of Tsc13p, the enoyl reductase of the yeast microsomal fatty acid elongating system. J. Exp. Bot. 55 (2004) 543–545. [DOI] [PMID: 14673020]
3.	Kvam, E., Gable, K., Dunn, T.M. and Goldfarb, D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16 (2005) 3987–3998. [DOI] [PMID: 15958487]
4.	Zheng, H., Rowland, O. and Kunst, L. Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. Plant Cell 17 (2005) 1467–1481. [DOI] [PMID: 15829606]

[EC 1.3.1.93 created 2012]