Cyclopropane-fatty-acyl-phospholipid synthase
In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + phospholipid olefinic fatty acid S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
Thus, the two substrates of this enzyme are S-adenosyl methionine and phospholipid olefinic fatty acid, whereas its two products are S-adenosylhomocysteine and phospholipid cyclopropane fatty acid.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (cyclizing). Other names in common use include cyclopropane synthetase, unsaturated-phospholipid methyltransferase, cyclopropane synthase, cyclopropane fatty acid synthase, cyclopropane fatty acid synthetase, and CFA synthase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1KP9, 1KPG, 1KPH, 1KPI, 1L1E, and 1TPY.
References
- Chung AE and Law JH (1964). "Cyclopropane fatty acid synthetase: Partial purification and properties". Biochemistry 3 (7): 967–974. doi:10.1021/bi00895a021. PMID 14214089.
- Zalkin H, Law JH and Goldfine H (1963). "Enzymatic synthesis of cyclopropane fatty acids catalyzed by bacterial extracts". J. Biol. Chem. 238: 1242–1248. PMID 14003136.
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