Ontology highlight
ABSTRACT:
SUBMITTER: Sheen P
PROVIDER: S-EPMC3391041 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Sheen Patricia P Ferrer Patricia P Gilman Robert H RH Christiansen Gina G Moreno-Román Paola P Gutiérrez Andrés H AH Sotelo Jun J Evangelista Wilfredo W Fuentes Patricia P Rueda Daniel D Flores Myra M Olivera Paula P Solis José J Pesaresi Alessandro A Lamba Doriano D Zimic Mirko M
The American journal of tropical medicine and hygiene 20120701 1
Pyrazinamidase of Mycobacterium tuberculosis catalyzes the conversion of pyrazinamide to the active molecule pyrazinoic acid. Reduction of pyrazinamidase activity results in a level of pyrazinamide resistance. Previous studies have suggested that pyrazinamidase has a metal-binding site and that a divalent metal cofactor is required for activity. To determine the effect of divalent metals on the pyrazinamidase, the recombinant wild-type pyrazinamidase corresponding to the H37Rv pyrazinamide-susce ...[more]