Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase

Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase
Identifiers
EC number 4.2.1.134
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

a very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] a very-long-chain trans-2,3-dehydroacyl-[acyl-carrier protein] + H2O

This is the third component of the elongase.

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. (2008). "The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development". Proc. Natl. Acad. Sci. USA. 105: 14727–14731. PMC 2567193Freely accessible. PMID 18799749. doi:10.1073/pnas.0805089105.
  2. Kihara, A.; Sakuraba, H.; Ikeda, M.; Denpoh, A.; Igarashi, Y. (2008). "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. PMID 18272525. doi:10.1074/jbc.m708993200.
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