Chlorocob(II)alamin Formation Which Enhances the Thiol Oxidase Activity of the B₁₂-Trafficking Protein CblC.

ABSTRACT: CblC is a chaperone that catalyzes removal of the β-axial ligand of cobalamin (or B₁₂), generating cob(II)alamin in an early step in the cofactor trafficking pathway. Cob(II)alamin is subsequently partitioned to support cellular needs for the synthesis of active cobalamin cofactor derivatives. In addition to the β-ligand transferase activity, the Caenorhabdiitis elegans CblC (ceCblC) and clinical R161G/Q variants of the human protein exhibit robust thiol oxidase activity, converting glutathione to glutathione disulfide while concomitantly reducing O₂ to H₂O₂. The chemical efficiency of the thiol oxidase side reaction during ceCblC-catalyzed dealkylation of alkylcobalamins is noteworthy in that it effectively scrubs ambient ox

SUBMITTER: Li Z 

PROVIDER: S-EPMC7607454 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature