(5R)-carbapenam-3-carboxylate synthase (CarC)

(5R)-carbapenam-3-carboxylate synthase, commonly known as CarC, is a critical enzyme in the biosynthetic pathway of carbapenem antibiotics, such as those produced by the Gram-negative bacterium Pectobacterium carotovorum (UniProt: P31976). It belongs to the superfamily of mononuclear ferrous iron and 2-oxoglutarate-dependent oxygenases (PubMed: 10764578). CarC is unique because it catalyzes two distinct chemical transformations: the epimerization of the (5S)-carbapenam-3-carboxylate intermediate to its (5R) isomer and the subsequent desaturation to form the carbapenem nucleus (PubMed: 15103024). This enzyme is essential for creating the potent beta-lactam core that characterizes carbapenem antibiotics, which are vital for treating multi-drug resistant bacterial infections. While CarC is not a traditional therapeutic target for drug inhibition, it is a major focus of metabolic engineering and synthetic biology efforts aimed at developing new antimicrobial agents or improving the yield of existing ones (PubMed: 21859135). Its complex mechanism involving radical intermediates also makes it a significant model for studying oxygen-dependent enzymatic reactions.

Other names

Carbapenem synthase1-carbapenem-3-carboxylate synthaseL-proline-dependent carbapenem synthaseCarC proteinCarbapenam-3-carboxylate synthase