Analysis of catalytic residues in enzyme active sites.
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.
Bartlett
Gail J
GJ
Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
Porter
Craig T
CT
Borkakoti
Neera
N
Thornton
Janet M
JM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D017124:Conserved Sequence; D030562:Databases, Protein; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D012997:Solvents; D013329:Structure-Activity Relationship
D000596:Amino Acids; D004798:Enzymes; D012997:Solvents