Binding kinetics overview

Additional information <1, 7-9, 12-17, 21> (<7> inhibitory effect of phosphonate analogues of 1,3-diphosphoglycerate, overview [49] <21> no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate [70] <13> double-inhibition studies, kinetics, modeling of inhibitor binding, e.g. phosphate [55] <13> enzyme is regulated by multivalent anions, overview [55] <8> no inhibition by Hg [25] <1,7,9,12-17> yeast enzyme is insensitive to thiol reagents [17]) [17, 25, 49, 55, 70]... 

Previous sections of this chapter have focused on developing general principles for enzyme-catalyzed reactions based on analysis of single-substrate enzyme systems. Yet the majority of biochemical reactions involve multiple substrates and products. With multiple binding steps, competitive and uncompetitive binding interactions, and allosteric and covalent activations and inhibitions possible, the complete set of possible kinetic mechanisms is vast. For extensive treatments on a great number of mechanisms, we point readers to Segel s book [183], Here we review a handful of two-substrate reaction mechanisms, with detailed analysis of the compulsory-order ternary mechanism and a cursory overview of several other mechanisms. 

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