EC 4.2.1.134 - Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase

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IntEnz Enzyme Nomenclature
EC 4.2.1.134

Names

Accepted name:
very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
Other names:
PHS1 (gene name)
PAS2 (gene name)
Systematic name:
very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase

Reaction

Comments:

This is the third 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 1.3.1.93, very-long-chain enoyl-CoA reductase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102343 , GO:0102344 , GO:0102345 , GO:0102158
UniProtKB/Swiss-Prot: (24) [show] [UniProt]

References

  1. Bach, L., Michaelson, L. V., Haslam, R., Bellec, Y., Gissot, L., Marion, J., Da Costa, M., Boutin, J. P., Miquel, M., Tellier, F., Domergue, F., Markham, J. E., Beaudoin, F., Napier, J. A., Faure, J. D.
    The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development.
    Proc. Natl. Acad. Sci. U.S.A. 105: 14727-14731 (2008). [PMID: 18799749]
  2. Kihara, A., Sakuraba, H., Ikeda, M., Denpoh, A., Igarashi, Y.
    Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation.
    J. Biol. Chem. 283: 11199-11209 (2008). [PMID: 18272525]

[EC 4.2.1.134 created 2012, modified 2014]