Transition state analogs for thiamin pyrophosphate-dependent enzymes.
作者： J A Gutowski , G E Lienhard
DOI: 10.1016/S0021-9258(17)33570-6
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摘要: Many of the transition states that are formed from thiamin pyrophosphate in enzymic reactions expected to have structures which thiazolium ring has lost most its positive charge. We synthesized thiazolone unphosphorylated compound. The sulphur-containing is uncharged, and thus compound resembles these states. In agreement with prediction state theory reaction rates, binds Escherichia coli pyruvate dehydrogenase complex (EC 1.2.7.1) much more strongly than itself. An upper limit for value dissociation constant, calculated extent inactivation enzyme by a low concentration pyrophosphate, 5 X 10(-10) M at 3 degrees 0.5 mM MgCl2/10 potassium phosphate, pH 6.6. constant under similar conditions about 10(-5) M. kinetics first order respect both pyrophosphate; second rate 5.7 10(5) M-1 min-1 analysis decrease rates caused indicates coenzyme sites. also thiothiazolone obtained very results this
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