Bacterial Hydratases Involved in Steroid Side Chain Degradation Have Distinct Substrate Specificities.

ABSTRACT: Actinobacterial MaoC family enoyl coenzyme A (CoA) hydratases catalyze the addition of water across the double bond of CoA esters during steroid side chain catabolism. We determined that heteromeric MaoC type hydratases, exemplified by ChsH1-ChsH2_Mtb of Mycobacterium tuberculosis and CasM-CasO_Rjost from Rhodococcus jostii RHA1, are specific toward a 3-carbon side chain steroid metabolite, consistent with their roles in the last β-oxidation cycle of steroid side chain degradation. Hydratases containing two fused MaoC domains are responsible for the degradation of longer steroid side chains. These hydratases, encoded in the cholesterol degradation gene clusters of M. tuberculosis and R. jostii RHA1, have broad specificity and were able to catalyze the hydration o

SUBMITTER: Schroeter KL 

PROVIDER: S-EPMC9491828 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature