Biology:Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase
From HandWiki
| Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase | |||||||||
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| 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 | ||||||||
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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] [math]\displaystyle{ \rightleftharpoons }[/math] a very-long-chain trans-2,3-dehydroacyl-[acyl-carrier protein] + H2O
This is the third component of the elongase.
References
- ↑ Bach, L.; Michaelson, L.V.; Haslam, R.; Bellec, Y.; Gissot, L.; Marion, J.; Da Costa, M.; Boutin, J.P. et al. (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. doi:10.1073/pnas.0805089105. PMID 18799749.
- ↑ 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. doi:10.1074/jbc.m708993200. PMID 18272525.
External links
- Very-long-chain+(3R)-3-hydroxyacyl-(acyl-carrier+protein)+dehydratase at the US National Library of Medicine Medical Subject Headings (MeSH)
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