In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) is an enzyme that catalyzes the chemical reaction
cyclopropane-fatty-acyl-phospholipid synthase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.79 | ||||||||
CAS no. | 51845-48-8 | ||||||||
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 | ||||||||
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- 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
editAs 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
edit- Chung AE, 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; Goldfine H (1963). "Enzymatic synthesis of cyclopropane fatty acids catalyzed by bacterial extracts". J. Biol. Chem. 238 (4): 1242–1248. doi:10.1016/S0021-9258(18)81170-X. PMID 14003136.