Abstract
THE ACTION OF AMINOBENZYLTHIAZOLIUM SALTS ON THIAMINE DESTRUCTION BY THE CHASTEK PARALYSIS ENZYME
Highlights
The increased destruction in the three instances yields a calculated activation of 17.5, 41.0, and 50.0 per cent, respectively. This activation has been observed in numerous other experiments with the same compound and is substantiated by the results obtained with the m-aminobenzyl-amethylthiazolium compound in a large variety of experiments
It seems reasonable to assume in this case that the presence of two methyl groups introduces a degree of steric hindrance sufficient to decrease to a measurable degree the binding of the inhibitor to the enzyme in spite of the possible free rotation of the thiazole ring in relation to the benzyl ring
The previous finding that thiamine destruction by the Chastek paralysis enzyme of fish tissues is inhibited by o-aminobenzyl-(3)-4-methylthiazolium chloride has been confirmed
Summary
In the same experiment a Michaelis constant of 8.31 X 10m5 mole per liter was obtained for the enzyme-substrate (thiamine) complex With this quantitative evidence of specific and competitive inhibitory activity, this analogue which so closely resembles the structural pattern of the vitamin was selected as the point of demarcation for the more detailed analysis of the essential characteristics of an inhibitor molecule. The compounds selected for this study included quaternary benzyl, and o-, m-, and p-aminobenzyl derivatives of 2-, or 4-methyl-, or 2,4-dimethylthiazole Their synthesis has been readily accomplished (4) by the method of Clarke (5) and it is the purpose of this paper to record the results of their use in connection with the thiamine-destroying enzyme.
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