(Redirected from
Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase)
| Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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-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
This is the third component of the elongase.
References
- ^ 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.
- ^ 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.
External links
- Very-long-chain+(3R)-3-hydroxyacyl-CoA+dehydratase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
Very-long-chain (3R)-3-hydroxyacyl-(acyl-carrier protein) dehydratase)
| Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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-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
This is the third component of the elongase.
References
- ^ 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.
- ^ 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.
External links
- Very-long-chain+(3R)-3-hydroxyacyl-CoA+dehydratase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)