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• W2043886357 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." @default.
• W2043886357 created "2016-06-24" @default.
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• W2043886357 date "2002-11-01" @default.
• W2043886357 modified "2023-10-10" @default.
• W2043886357 title "Analysis of Catalytic Residues in Enzyme Active Sites" @default.
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• W2043886357 doi "https://doi.org/10.1016/s0022-2836(02)01036-7" @default.
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