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  • Title: Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.
    Author: Pedretti M, Fernández-Rodríguez C, Conter C, Oyenarte I, Favretto F, di Matteo A, Dominici P, Petrosino M, Martinez-Chantar ML, Majtan T, Astegno A, Martínez-Cruz LA.
    Journal: Sci Rep; 2024 Apr 23; 14(1):9364. PubMed ID: 38654065.
    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 substrates. Comparative analysis with the human enzyme and counterparts from other pathogens revealed distinct structural features within the primary enzyme cavities. Specifically, a distinctly folded entrance loop could potentially modulate the access of substrates and/or inhibitors to the catalytic site. Our findings offer significant insights into the structural evolution of CGL enzymes across different pathogens and provide novel opportunities for developing specific inhibitors targeting PaCGL.
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