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

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (EC 4.2.1.134, PHS1 (gene), PAS2 (gene)) is an enzyme with systematic name very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase.[1][2] This enzyme catalyses the following chemical reaction

a very-long-chain (3R)-3-hydroxyacyl-CoA a very-long-chain trans-2,3-dehydroacyl-CoA + H2O
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
Identifiers
EC no.4.2.1.134
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

This is the third component of the elongase.

References

  1. Bach L, Michaelson LV, Haslam R, Bellec Y, Gissot L, Marion J, Da Costa M, Boutin JP, Miquel M, Tellier F, Domergue F, Markham JE, Beaudoin F, Napier JA, Faure JD (September 2008). "The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development". Proceedings of the National Academy of Sciences of the United States of America. 105 (38): 14727–31. doi:10.1073/pnas.0805089105. PMC 2567193. PMID 18799749.
  2. Kihara A, Sakuraba H, Ikeda M, Denpoh A, Igarashi Y (April 2008). "Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation". The Journal of Biological Chemistry. 283 (17): 11199–209. doi:10.1074/jbc.m708993200. PMID 18272525.
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