期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 166, 期 -, 页码 182-189出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2016.11.016
关键词
Urease inhibition; Catechol; Nickel; Kinetic measurements; X-ray crystallography
资金
- University of Bologna
- CIRMMP (Consorzio Interuniversitario di Risonanze Magnetiche di Metallo-Proteine)
- Specialty Fertilizer Products (Leawood, KS, USA)
- European Molecular Biology Laboratory (EMBL, Petra III, Hamburg, Germany) [MX-333]
Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 10(15) 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 1.50 angstrom resolution, reveals the structural details of the enzyme inhibition. (C) 2016 Elsevier Inc. All rights reserved.
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