Erythronolide synthase

In enzymology, an erythronolide synthase 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.

Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , and.