Analysis of catalytic residues in enzyme active sites |
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Authors: | Bartlett Gail J Porter Craig T Borkakoti Neera Thornton Janet M |
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Institution: | Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK. |
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Abstract: | We present an analysis of the residues directly involved in catalysis in 178 enzyme active sites. Specific criteria were derived to define a catalytic residue, and used to create a catalytic residue dataset, which was then analysed in terms of properties including secondary structure, solvent accessibility, flexibility, conservation, quaternary structure and function. The results indicate the dominance of a small set of amino acid residues in catalysis and give a picture of a general active site environment. It is hoped that this information will provide a better understanding of the molecular mechanisms involved in catalysis and a heuristic basis for predicting catalytic residues in enzymes of unknown function. |
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Keywords: | enzyme active site catalysis amino acid residue enzyme function |
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