Inactivation of urease by catechol: Kinetics and structure

J Inorg Biochem. 2017 Jan:166:182-189. doi: 10.1016/j.jinorgbio.2016.11.016. Epub 2016 Nov 9.

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.

Keywords: Catechol; Kinetic measurements; Nickel; Urease inhibition; X-ray crystallography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins* / antagonists & inhibitors
  • Bacterial Proteins* / chemistry
  • Canavalia / enzymology*
  • Catechols* / antagonists & inhibitors
  • Catechols* / chemistry
  • Models, Molecular*
  • Plant Proteins* / antagonists & inhibitors
  • Plant Proteins* / chemistry
  • Sporosarcina / enzymology*
  • Urease* / antagonists & inhibitors
  • Urease* / chemistry

Substances

  • Bacterial Proteins
  • Catechols
  • Plant Proteins
  • Urease
  • catechol