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Mycobacterium tuberculosis puromycin hydrolase displays a prolyl oligopeptidase fold and an acyl aminopeptidase activity

Proteins. 2021-01; 
YuanHao Zhao, Qiaoli Feng, Xiao Zhou, Yan Zhang, Maxwell Lukman, Jie Jiang, David Ruiz-Carrillo
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Bacterial Expression … The cDNA of MtPMH was synthetically generated (GenScript/Suzhou/China) and cloned into the bacterial expression vector pET28a + using the Nde-I and Xho-I restrictions sites … Get A Quote

摘要

Puromycin-hydrolizing peptidases have been described as members of the prolyl oligopeptidase peptidase family. These enzymes are present across all domains of life but still little is known of the homologs found in the pathogenic bacterium Mycobacterium tuberculosis. The crystal structure of a M. tuberculosis puromycin hydrolase peptidase has been determined at 3 Angstrom resolution, revealing a conserved prolyl oligopeptidase fold, defined by α/β-hydrolase and β-propeller domains with two distinctive loops that occlude access of large substrates to the active site. The enzyme displayed amino peptidase activity with a substrate specificity preference for hydrophobic residues in the decreasing order of phenyl... More

关键词

amino acyl peptidase, mycobacterium tuberculosis, prolyl Oligopeptidase, puromycin, puromycin hydrolase, x-ray structure