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 par- ticular, 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 1.50 Å resolution, reveals the struc- tural details of the enzyme inhibition.
Inactivation of urease by catechol: Kinetics and structure / Mazzei, Luca; Cianci, Michele; Musiani, Francesco; Lente, Gábor; Palombo, Marta; Ciurli, Stefano. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - ELETTRONICO. - 166:(2017), pp. 182-189. [10.1016/j.jinorgbio.2016.11.016]
Inactivation of urease by catechol: Kinetics and structure
CIANCI, MICHELE;
2017-01-01
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 par- ticular, 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 1.50 Å resolution, reveals the struc- tural details of the enzyme inhibition.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
