title: Plasticity of enzyme active sites.
abstract: The expectation is that any similarity in reaction chemistry shared by enzyme homologues is mediated by common functional groups conserved through evolution. However, detailed enzyme studies have revealed the flexibility of many active sites, in that different functional groups, unconserved with respect to position in the primary sequence, mediate the same mechanistic role. Nevertheless, the catalytic atoms might be spatially equivalent. More rarely, the active sites have completely different locations in the protein scaffold. This variability could result from: (1) the hopping of functional groups from one position to another to optimize catalysis; (2) the independent specialization of a low-activity primordial enzyme in different phylogenetic lineages; (3) functional convergence after evolutionary divergence; or (4) circular permutation events.
authors.affiliation: Biochemistry and Molecular Biology Department, University College London, Gower Street, London, UK WC1E 6BT.
authors.forename: Annabel E
authors.initials: AE
authors.lastname: Todd
authors.forename: Christine A
authors.initials: CA
authors.lastname: Orengo
authors.forename: Janet M
authors.initials: JM
authors.lastname: Thornton
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D004798:Enzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019143:Evolution, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D004798:Enzymes