Identification of dehydrogenase, hydratase, and aldolase responsible for the propionyl residue removal in degradation of cholic acid C-17 side chain in <i>Comamonas testosteroni</i> TA441.

ABSTRACT: Bacterial steroid degradation is gaining attention for its diverse roles, such as Mycobacterium tuberculosis's reliance on the degradation of the C17 side chain of cholesterol for survival in host environments. ORF40-44 of Comamonas testosteroni TA441, previously characterized for its A-, B-, C-, and D-ring cleavage pathways, were hypothesized to correspond to the igr operon of M. tuberculosis, encoding the dehydrogenase ChsE1E2, hydratase ChsH1H2_MaoC, and aldolase Ltp2 ChsH2_DUF35, responsible for propionyl residue removal in the degradation of the cholic acid C17 side chain. However, low amino acid identity between the corresponding enzymes precluded functional assignment without experimental evidence. In this study, we generated gene-disr

SUBMITTER: Horinouchi M 

PROVIDER: S-EPMC12502768 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature