This work provides a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the relationships between the structural Features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme. In addition, the recently determined structure of a complex between urease and a transition state analogue is discussed as it leads to a novel, thought-provoking proposal for the enzyme mechanism. (C) 1999 Elsevier Science S.A. All rights reserved
The biochemical properties of the metal ions in a series of nickel enzymes are briefly reviewed. In ...
Urease, the most efficient enzyme known, contains an essential dinuclear NiII cluster in the active ...
Urease, the most efficient enzyme so far discovered, depends on the presence of nickel ions in the c...
This work provides a comprehensive critical summary of urease spectroscopy, crystallography, inhibit...
Urease is the enzyme that catalyzes the hydrolysis of urea as the last step of organic nitrogen mine...
This review is an attempt to retrace the chronicle that starts from the discovery of the role of nic...
Although the discovery of urease as the first enzyme for which nickel is essential for activity date...
Urease was the first enzyme to be crystallized and shown to be a protein. Some 50 years after its cr...
The article defines the development of our present understanding of the urease molecule. It describe...
Abstract The viability of different mechanisms of catalysis and inhibition of the nickel-containing ...
Transition metals are both essential to enzymatic catalysis and limited in environmental availabilit...
The double face of nickel, being both a toxic element for living organisms and a necessary metal for...
Background: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mineralizati...
AbstractBackground: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mine...
The biochemical properties of the metal ions in a series of nickel enzymes are briefly reviewed. In ...
Urease, the most efficient enzyme known, contains an essential dinuclear NiII cluster in the active ...
Urease, the most efficient enzyme so far discovered, depends on the presence of nickel ions in the c...
This work provides a comprehensive critical summary of urease spectroscopy, crystallography, inhibit...
Urease is the enzyme that catalyzes the hydrolysis of urea as the last step of organic nitrogen mine...
This review is an attempt to retrace the chronicle that starts from the discovery of the role of nic...
Although the discovery of urease as the first enzyme for which nickel is essential for activity date...
Urease was the first enzyme to be crystallized and shown to be a protein. Some 50 years after its cr...
The article defines the development of our present understanding of the urease molecule. It describe...
Abstract The viability of different mechanisms of catalysis and inhibition of the nickel-containing ...
Transition metals are both essential to enzymatic catalysis and limited in environmental availabilit...
The double face of nickel, being both a toxic element for living organisms and a necessary metal for...
Background: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mineralizati...
AbstractBackground: Urease catalyzes the hydrolysis of urea, the final step of organic nitrogen mine...
The biochemical properties of the metal ions in a series of nickel enzymes are briefly reviewed. In ...
Urease, the most efficient enzyme known, contains an essential dinuclear NiII cluster in the active ...
Urease, the most efficient enzyme so far discovered, depends on the presence of nickel ions in the c...