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
| erythronolide synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.94 | ||||||||
| CAS number | 87683-77-0 | ||||||||
| 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 | ||||||||
| |||||||||
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, Nakagawa A (1981). "Biosynthesis of 16-membered macrolide antibiotics". Antibiotics. 4: 175–192. doi:10.1007/978-3-642-67724-3_8.
- Roberts G, Leadley PF (1984). "Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity in Streptomyces erythreus". Biochem. Soc. Trans. 12: 642–643.