Erythronolide synthase

From Wikipedia, the free encyclopedia

In enzymology, an erythronolide synthase (EC 2.3.1.94) is an enzyme that catalyzes the chemical reaction

6 malonyl-CoA + propanoyl-CoA $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 2.3.1.94
BRENDA references for 2.3.1.94 (Recommended.)
PubMed references for 2.3.1.94
PubMed Central references for 2.3.1.94
Google Scholar references for 2.3.1.94
Omura S and Nakagawa A (1981). "Biosynthesis of 16-membered macrolide antibiotics". Antibiotics 4: 175–192.
Roberts G and Leadley PF (1984). "Use of [3H]tetrahydrocerulenin to assay condensing enzyme activity in Streptomyces erythreus". Biochem. Soc. Trans. 12: 642–643.