Title of article
Analysis of Catalytic Residues in Enzyme Active Sites
Author/Authors
Gail J. Bartlett، نويسنده , , Craig T. Porter، نويسنده , , Neera Borkakoti، نويسنده , , Christine A. Orengo and Janet M. Thornton، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2002
Pages
17
From page
105
To page
121
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.
Keywords
enzyme active site , Catalysis , Amino acid residue , Enzyme function
Journal title
Journal of Molecular Biology
Serial Year
2002
Journal title
Journal of Molecular Biology
Record number
1242151
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