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- W1566165927 abstract "Abstract Zinc acts as catalytic metal center in a large variety of enzymes belonging to all functional classes. Basically, zinc functions as a Lewis acid center that polarizes and properly orients the substrate in the catalytic cleft of the enzyme, and confers to the site the structural and electronic properties competent for catalysis. In the zinc hydrolases, which are the most important class of zinc enzymes, the metal also assists the nucleophilic attack eventually exreted on the substrate by an active site group. Indeed, such a group is most often a Zn‐bound hydroxide. This article summarizes the main structural and mechanistic features of a number of zinc enzymes whose function has been elucidated in detail through structural (X‐ray) and spectroscopic (UV–vis and NMR) techniques. The latter were most often carried out on metal‐substituted species in which Zn 2+ was replaced with another metal possessing useful electronic and magnetic properties, most often Co 2+ . Particular focus has been put on the structure–function relationships in zinc‐containing peptidases and phosphatases, which carry out the hydrolysis of the CN and PO bond in peptides and phosphate esters, respectively. Moreover, the active site structure and catalytic mechanism of carbonic anhydrase, which is an important enzyme responsible for the reversible hydration of carbon dioxide, and of superoxide dismutase and alcohol dehydrogenase, which are redox enzymes of great physiological relevance, are also described. The contributions to the comprehension of enzyme function obtained from investigations of low molecular weight coordination compounds mimicking the active site features have been highlighted." @default.
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- W1566165927 date "2002-12-13" @default.
- W1566165927 modified "2023-10-12" @default.
- W1566165927 title "Zinc Enzymes and Models" @default.
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- W1566165927 doi "https://doi.org/10.1002/0471227617.eoc205" @default.
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