Background: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen
mineralization, using a bimetallic nickel centre. The role of the active site metal ions and …

The structure of Bacillus pasteurii urease (BPU) inhibited with phosphate was solved and
refined using synchrotron X-ray diffraction data from a vitrified crystal (1.85 Å resolution …

The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly
ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic …

The viability of different mechanisms of catalysis and inhibition of the nickel-containing
enzyme urease was explored using the available high-resolution structures of the enzyme …

Urease, a nickel-dependent metalloenzyme, is synthesized by plants, some bacteria, and
fungi. It catalyzes the hydrolysis of urea into ammonia and carbon dioxide. Although the …

The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved
and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å …

Cys319 is located on a mobile flap covering the active site of Klebsiella aerogenes urease
but does not play an essential role in catalysis. Four urease variants altered at position C319 …

This work provides a comprehensive critical summary of urease spectroscopy,
crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis …

Urease, the most efficient enzyme known, contains an essential dinuclear NiII cluster in the
active site. It catalyzes the hydrolysis of urea, inducing a rapid pH increase that has negative …

Urease, the first enzyme to be crystallized, contains a dinuclear nickel metallocenter that
catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural …