Analysis of catalytic residues in enzyme active sites.

by: GJ Bartlett, CT Porter, N Borkakoti, JM Thornton

J Mol Biol, Vol. 324, No. 1. (15 November 2002), pp. 105-121.

View FullText article

Pubmed, Hubmed

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

baaden, gbart, nickolay, sriram_s, siebertm

Find related articles with these CiteULike tags

aa-propensity, active, active_sites, analysis, catalytic, cat_res, enzyme, enzymes, no-tag, residue-conservation, residues, sites, structure-function

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.

@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}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {active, analysis, catalytic, enzyme, residues, sites}, month = {November}, number = {1}, pages = {105--121}, posted-at = {2007-05-14 10:55:17}, priority = {2}, title = {Analysis of catalytic residues in enzyme active sites.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12421562}, volume = {324}, year = {2002} }

RIS record

TY - JOUR ID - citeulike:308565 L3 - citeulike-article-id:308565 TI - Analysis of catalytic residues in enzyme active sites. JF - J Mol Biol VL - 324 IS - 1 SP - 105 EP - 121 AD - Department of Biochemistry and Molecular Biology, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK. SN - 0022-2836 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. KW - active KW - analysis KW - catalytic KW - enzyme KW - residues KW - sites 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 -

RIS BibTeX