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10.1016/j.bioorg.2014.07.001 http://scihub22266oqcxt.onion/10.1016/j.bioorg.2014.07.001 C4256097!4256097!25092608     free     free     free       Bioorg+Chem 2014 ; 57 (ä): 206-12 Nephropedia Template TP {{tp|p=25092608|t=2014. Reflections on the Catalytic Power of a TIM-Barrel |pdf=|usr=}}{{25092608}} gab.com Text Reflections on the Catalytic Power of a TIM-Barrel JO: Bioorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=25092608 #FOAvip The TIM-barrel fold is described and its propagation throughout the enzyme universe noted. The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) Electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an ?-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or D-glyceraldehyde 3-phosphate (DGAP). (b) The engineering of loop 3 to give the monomeric variant monoTIM and the structure and catalytic properties of this monomer. (c) The interaction between loops 6, 7 and 8 and the phosphodianion of DHAP or DGAP. (d) The mechanism by which a ligand-gated conformational change, dominated by motion of loops 6 and 7, activates TIM for catalysis of deprotonation of DHAP or DGAP. (e) The conformational plasticity of TIM, and the utilization of substrate binding energy to ?mold? the distorted active site loops of TIM mutants into catalytically active enzymes. The features of the TIM-barrel fold that favor effective protein catalysis are discussed. Twit Text FOAVip Reflections on the Catalytic Power of a TIM-Barrel ????Bioorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=25092608 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25092608 #FOAvip English Wikipedia <ref>{{Cite pmid|25092608}}</ref> Reflections on the Catalytic Power of a TIM-Barrel #MMPMID25092608 Richard JP; Zhai X; Malabanan MM Bioorg Chem 2014[Dec]; 57 (ä): 206-12 PMID25092608show ga The TIM-barrel fold is described and its propagation throughout the enzyme universe noted. The functions of the individual front loops of the eponymous TIM-barrel of triosephosphate isomerase are presented in a discussion of: (a) Electrophilic catalysis, by amino acid side chains from loops 1 and 4, of abstraction of an ?-carbonyl hydrogen from substrate dihydroxyacetone phosphate (DHAP) or D-glyceraldehyde 3-phosphate (DGAP). (b) The engineering of loop 3 to give the monomeric variant monoTIM and the structure and catalytic properties of this monomer. (c) The interaction between loops 6, 7 and 8 and the phosphodianion of DHAP or DGAP. (d) The mechanism by which a ligand-gated conformational change, dominated by motion of loops 6 and 7, activates TIM for catalysis of deprotonation of DHAP or DGAP. (e) The conformational plasticity of TIM, and the utilization of substrate binding energy to ?mold? the distorted active site loops of TIM mutants into catalytically active enzymes. The features of the TIM-barrel fold that favor effective protein catalysis are discussed. äReflections on the Catalytic Power of a TIM-Barrel (epmc).pdf DeepDyve Pubget Overpricing