Plasticity of enzyme active sites. Export

@article{Todd02, 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.}, author = {Todd, A. E. and Orengo, C. A. and Thornton, J. M.}, citeulike-article-id = {388913}, journal = {Trends Biochem Sci}, keywords = {active\_sites, enzyme, plasticity}, number = {8}, pages = {419--26}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {Plasticity of enzyme active sites.}, volume = {27}, year = {2002} }

TY - JOUR ID - Todd02 L3 - citeulike-article-id:388913 N2 - 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. IS - 8 JF - Trends Biochem Sci EP - 26 TI - Plasticity of enzyme active sites. VL - 27 SP - 419 KW - active_sites KW - enzyme KW - plasticity AU - Todd, AE AU - Orengo, CA AU - Thornton, JM PY - 2002/// ER -