Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms
Coordination Chemistry Reviews, 1999•Elsevier
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.
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.
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.
Elsevier
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