2-oxopropyl-CoM reductase (carboxylating) (2-KPCC)

2-oxopropyl-CoM reductase (carboxylating) (abbreviated 2-KPCC) is a bacterial oxidoreductase enzyme, formally classified under EC 1.8.1.5, that catalyzes the conversion of 2-oxopropyl-coenzyme M (2-oxopropyl-CoM) to acetoacetate, free coenzyme M, and NADPH. It is a member of the NADPH:disulfide oxidoreductase family, which includes glutathione reductase and thioredoxin reductase, but is unique in its ability to mediate both reductive cleavage of a thioether bond and subsequent carboxylation. This enzyme participates in the microbial pathway for catabolism of propylene in species like Xanthobacter autotrophicus, but has no known therapeutic, disease-modifying, or biomarker role in human health or disease. Its structure reveals an FAD-containing, DSOR-family fold with an adapted active site specialized for its unique chemistry[1][2][3][4][8].

Other names

NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylaseNADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase2-mercaptoethanesulfonate, acetoacetate:NADP+ oxidoreductase (decarboxylating)2-ketopropyl-CoM oxidoreductase/carboxylase

Catalyzes reductive cleavage of thioether linkage in 2-oxopropyl-CoM, then carboxylates the cleavage product to yield acetoacetate and free coenzyme M[2][3][8]