title: Functionally and structurally relevant residues of enzymes: are they segregated or overlapping?
abstract: There is a delicate balance between stability and flexibility needed for enzyme function. To avoid undesirable alteration of the functional properties during the evolutionary optimization of the structural stability under certain circumstances, and vice versa, to avoid unwanted changes of stability during the optimization of the functional properties of proteins, common sense would suggest that parts of the protein structure responsible for stability and parts responsible for function developed and evolved separately. This study shows that nature did not follow this anthropomorphic logic: the set of residues involved in function and those involved in structural stabilization of enzymes are rather overlapping than segregated.
authors.affiliation: Biological Research Center, Institute of Enzymology, Hungarian Academy of Sciences, PO Box 7, H-1518 Budapest, Hungary.
authors.forename: Csaba
authors.initials: C
authors.lastname: Magyar
authors.forename: Eva
authors.initials: E
authors.lastname: Tüdos
authors.forename: István
authors.initials: I
authors.lastname: Simon
mesh_terms: D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D019295:Computational Biology; D030562:Databases, Protein; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D004798:Enzymes