Zinc enzymes

The number of zinc enzymes for which detailed structural and mechanistic data, including high resolution crystal structures, are available is increasing rapidly. The new finding continue to support the conclusion that the majority of zinc enzymes catalyze hydrolysis or closely related transfer react...

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Bibliographic Details
Published in:Current opinion in chemical biology 1998-04, Vol.2 (2), p.222-234
Main Author: Coleman, Joseph E
Format: Article
Language:English
Subjects:
Alkaline Phosphatase - chemistry
Binding Sites
Carbonic Anhydrases - chemistry
Carbonic Anhydrases - genetics
Endopeptidases - chemistry
Hydrogen Bonding
Metalloendopeptidases - chemistry
Models, Molecular
Type C Phospholipases - chemistry
Zinc - chemistry
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Summary:The number of zinc enzymes for which detailed structural and mechanistic data, including high resolution crystal structures, are available is increasing rapidly. The new finding continue to support the conclusion that the majority of zinc enzymes catalyze hydrolysis or closely related transfer reactions. In a protein environment, tetrahedral or 5-coordinate Zn 2+ is ideally suited to activate a coordinate water (frequently a Zn 2+— −OH) as a nucleophile attacking the carbonyl carbon of a peptide bond, the carbon of carbon dioxide or the phosphorus of a phosphate ester. Protein-bound Zn 2+ can function catalytically by forming mixed complexes with the substrate, either by expanding its coordination sphere or by exchanging a ligand. Formation of protein—Zn 2+—substrate bonds can position the substrate or polarize its electron distribution to facilitate further steps in the reaction.
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(98)80064-1