Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces.
作者： Xiang Zhai , Tina L. Amyes , John P. Richard
DOI: 10.1021/JA501103B
关键词:
摘要: Values of (kcat/Km)GAP for triosephosphate isomerase-catalyzed reactions (R)-glyceraldehyde 3-phosphate and kcat/KHPiKGA the substrate pieces glycolaldehyde HPO32– have been determined wild-type following TIM mutants: I172V, I172A, L232A, P168A (TIM from Trypanosoma brucei brucei); a 208-TGAG 208-YGGS loop 7 replacement mutant (L7RM, chicken muscle); and, Y208T, Y208S, Y208A, Y208F S211A (yeast TIM). A superb linear logarithmic correlation, with slope 1.04 ± 0.03, is observed between kinetic parameters most enzymes, positive deviations L232A L7RM. The unit shows that mutations result in an identical change activation barriers catalyzed whole pieces, so two transition states are stabilized by similar interactions protein catalyst. This consistent role dianions as active spectators, which hold catalytical...
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