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

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


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



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, very-long-chain 3-oxoacyl-CoA synthase, EC, very-long-chain 3-oxoacyl-CoA reductase, and EC, 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: (29) [show] [UniProt]


  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 created 2012, modified 2014]