ExplorEnz: EC 4.2.1.134

Your query returned 1 entry. Printable version

4.2.1.134

Accepted name:

very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase

Reaction:

a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H₂O

Glossary:

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

Other name(s):

PHS1 (gene name); PAS2 (gene name)

Systematic name:

very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

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. and Faure, J.D. The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO₂ is essential and limiting for plant development. Proc. Natl. Acad. Sci. USA 105 (2008) 14727–14731. [DOI] [PMID: 18799749]

Kihara, A., Sakuraba, H., Ikeda, M., Denpoh, A. and 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 (2008) 11199–11209. [DOI] [PMID: 18272525]

[EC 4.2.1.134 created 2012, modified 2014]