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Publication Abstract from PubMed

Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 1015 times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50A resolution, reveals the structural details of the enzyme inhibition.

Inactivation of urease by catechol: Kinetics and structure.,Mazzei L, Cianci M, Musiani F, Lente G, Palombo M, Ciurli S J Inorg Biochem. 2016 Nov 9;166:182-189. doi: 10.1016/j.jinorgbio.2016.11.016. PMID:27888701^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.