This review is an attempt to retrace the chronicle that starts from the discovery of the role of
nickel as the essential metal ion in urease for the enzymatic catalysis of urea, a key step in …

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 …

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

Transition metals are both essential to enzymatic catalysis and limited in environmental
availability. These two biological facts have together driven organisms to evolve …

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 …

Department of Chemistry, Massachusetts Institute of Technology, Cambridge,
Massachusetts 02139 Received April 3, 1987; Revised Manuscript Received May 11, 1987 …

Approximately one-third of the known enzymes are metalloenzymes. The metal ions
promote a variety of reactions in these enzymes, including bond cleavage and formation …

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 …

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 …

The article defines the development of our present understanding of the urease molecule. It
describes physical and chemical properties of the enzyme, the interaction of inhibitors with …