Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.

ABSTRACT: The escalating drug resistance among microorganisms underscores the urgent need for innovative therapeutic strategies and a comprehensive understanding of bacteria's defense mechanisms against oxidative stress and antibiotics. Among the recently discovered barriers, the endogenous production of hydrogen sulfide (H₂S) via the reverse transsulfuration pathway, emerges as a noteworthy factor. In this study, we have explored the catalytic capabilities and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa (PaCGL), a multidrug-opportunistic pathogen chiefly responsible for nosocomial infections. In addition to a canonical L-cystathionine hydrolysis, PaCGL efficiently catalyzes the production of H₂S using L-cysteine and/or L-homocysteine as alternative s

SUBMITTER: Pedretti M 

PROVIDER: S-EPMC11039470 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature