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Inactivation of Urease by Catechol: Kinetics and Structure

Inactivation of Urease by Catechol: Kinetics and Structure

Luca Mazzei, Michele Cianci, Francesco Musiani, Gábor Lente, Marta Palombo, Stefano Ciurli

J Inorg Biochem. 2017 Jan;166:182-189.

PMID: 27888701

Abstract:

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 1.50Å resolution, reveals the structural details of the enzyme inhibition.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9002135-A	Urease from Canavalia ensiformis (Jack bean)		9002-13-5	Price

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