Analysis of catalytic residues in enzyme active sites. Export

@article{citeulike:308565, 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.}, address = {Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.}, author = {Bartlett, G. J. and Porter, C. T. and Borkakoti, N. and Thornton, J. M.}, citeulike-article-id = {308565}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12421562}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12421562}, day = {15}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {calatytic, enzyme, p1, props, protein, site}, month = {November}, number = {1}, pages = {105--121}, posted-at = {2006-03-02 02:19:36}, priority = {0}, title = {Analysis of catalytic residues in enzyme active sites.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12421562}, volume = {324}, year = {2002} }

TY - JOUR ID - citeulike:308565 L3 - citeulike-article-id:308565 N2 - 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. IS - 1 JF - J Mol Biol SN - 0022-2836 AD - Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK. EP - 121 TI - Analysis of catalytic residues in enzyme active sites. VL - 324 SP - 105 KW - calatytic KW - enzyme KW - p1 KW - props KW - protein KW - site AU - Bartlett, GJ AU - Porter, CT AU - Borkakoti, N AU - Thornton, JM PY - 2002/11/15/ UR - http://view.ncbi.nlm.nih.gov/pubmed/12421562 ER -