STUDIES ON ENZYMATIC SYNTHESIS OF COCARBOXYLASE IN ANIMAL TISSUE

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Abstract
Partly purified rat liver thiaminokinase (Y. Mano, Jour. Biochem., 47, 24 (1960)) is likely contaminated by other enzymes, by which the enzymic formation of thiamine diphosphate (TDP) from thiamine and adenosine triphosphate (ATP) was affected. ATPase and adenylate kinase decompose ATP as a P-donpr and yield inhibitory products, such as adenosine diphosphate and adenosine-5[image]-monophosphate. Acceleration by phosphoenolpyruvate of enzymic TDP formation is caused by contaminating pyruvate kinase according to the following reaction: 2 phosphoenolpyruvate + adenosine-5''-monophosphate[forward arrow] ATP + 2 pyruvate, whereby ATP is regenerated and an inhibitor, adenosine-5[image]-monophosphate is eliminated.