Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.

ABSTRACT: Mycobacterium tuberculosis virulence is highly metal-dependent with metal availability modulating the shift from the dormant to active states of M. tuberculosis infection. Rv0045c from M. tuberculosis is a proposed metabolic serine hydrolase whose folded stability is dependent on divalent metal concentration. Herein, we measured the divalent metal inhibition profile of the enzymatic activity of Rv0045c and found specific divalent transition metal cations (Cu²⁺  ≥ Zn²⁺  > Ni²⁺  > Co²⁺ ) strongly inhibited its enzymatic activity. The metal cations bind allosterically, largely affecting values for k_cat rather than K_M . Removal of the artificial N-terminal 6xHis-tag did not change the metal-dependent inhibition, indicating that

SUBMITTER: Bowles IE 

PROVIDER: S-EPMC8284577 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature