Biology:Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
From HandWiki
| Very-long-chain (3R)-3-hydroxyacyl-CoA 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-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
- ↑ "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. September 2008. doi:10.1073/pnas.0805089105. PMID 18799749. PMC 2567193. http://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1093&context=biochemfacpub.
- ↑ "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. April 2008. doi:10.1074/jbc.m708993200. PMID 18272525.
External links
- Very-long-chain+(3R)-3-hydroxyacyl-CoA+dehydratase at the US National Library of Medicine Medical Subject Headings (MeSH)
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