Erythronolide synthase
In enzymology, an erythronolide synthase (EC 2.3.1.94) is an enzyme that catalyzes the chemical reaction
- 6 malonyl-CoA + propanoyl-CoA
7 CoA + 6-deoxyerythronolide b
Thus, the two substrates of this enzyme are malonyl-CoA and propanoyl-CoA, whereas its two products are CoA and 6-deoxyerythronolide b.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:propanoyl-CoA malonyltransferase (cyclizing). Other names in common use include erythronolide condensing enzyme, and malonyl-CoA:propionyl-CoA malonyltransferase (cyclizing). This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1KEZ, 1MO2, 1PZQ, 1PZR, 2HG4, 2JU1, 2JU2, and 2QO3.
References
- Omura S and Nakagawa A (1981). "Biosynthesis of 16-membered macrolide antibiotics". Antibiotics 4: 175–192. doi:10.1007/978-3-642-67724-3_8.
- Roberts G and Leadley PF (1984). "Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity in Streptomyces erythreus". Biochem. Soc. Trans. 12: 642–643.
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|