Delta12-fatty acid dehydrogenase
| delta12-fatty acid dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.99.33 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a Delta12-fatty acid dehydrogenase (EC 1.14.99.33) is an enzyme that catalyzes the chemical reaction
- linoleate + 2AH + O2 crepenynate + 2A + H2O
where AH is either NADH or NADPH.
The 3 substrates of this enzyme are linoleate, 2AH, and O2, whereas its 3 products are crepenynate, 2A, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous.
This enzyme participates in linoleic acid metabolism.
Nomenclature[edit]
The systematic name of this enzyme class is linoleate, hydrogen-donor:oxygen oxidoreductase (Delta12-unsaturating). Other names in common use include
- crepenynate synthase and
- linoleate Delta12-fatty acid acetylenase (desaturase).
References[edit]
Further reading[edit]
- Banas A, Bafor M, Wiberg E, Lenman M, Ståhl U, Stymne S (1997). "Biosynthesis of an Acetylenic Fatty Acid in Microsomal Preparations from Developing Seeds of Crepis Alpina.". In Williams JP, Khan MU, Lem NW (eds.). Physiology, Biochemistry and Molecular Biology of Plant Lipids. Dordrecht: Springer. pp. 57–59. doi:10.1007/978-94-017-2662-7_18. ISBN 978-90-481-4784-7.
- Lee M, Lenman M, Banaś A, Bafor M, Singh S, Schweizer M, Nilsson R, Liljenberg C, Dahlqvist A, Gummeson PO, Sjödahl S, Green A, Stymne S (May 1998). "Identification of non-heme diiron proteins that catalyze triple bond and epoxy group formation". Science. 280 (5365): 915–8. doi:10.1126/science.280.5365.915. PMID 9572738.
