Cyclopropane-fatty-acyl-phospholipid synthase

{{infobox enzyme

| Name = cyclopropane-fatty-acyl-phospholipid synthase

| EC_number = 2.1.1.79

| CAS_number = 51845-48-8

| GO_code = 0008825

| image =

| width =

| caption =

}}

In enzymology, a cyclopropane-fatty-acyl-phospholipid synthase ({{EC number|2.1.1.79}}) is an enzyme that catalyzes the chemical reaction

:S-adenosyl-L-methionine + phospholipid olefinic fatty acid $\rightleftharpoons$ 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 {{PDB link|1KP9}}, {{PDB link|1KPG}}, {{PDB link|1KPH}}, {{PDB link|1KPI}}, {{PDB link|1L1E}}, and {{PDB link|1TPY}}.

References

{{cite journal |vauthors = Chung AE, Law JH | year = 1964 | title = Cyclopropane fatty acid synthetase: Partial purification and properties | journal = Biochemistry | volume = 3 | pages = 967–974 | doi = 10.1021/bi00895a021 | pmid=14214089 | issue = 7}}
{{cite journal |author1 = Zalkin H, Law JH |author2 =Goldfine H | year = 1963 | title = Enzymatic synthesis of cyclopropane fatty acids catalyzed by bacterial extracts | journal = J. Biol. Chem. | volume = 238 |issue =4 | pages = 1242–1248 |doi =10.1016/S0021-9258(18)81170-X |doi-access =free | pmid=14003136}}

Category:EC 2.1.1

Category:Enzymes of known structure