Dismutations and oxidoreductions

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Abstract
The properties and reactions of the triose, triose-phosphate and a-glycerophosphate mutases were studied. Their activities depended upon coenzyme I. They catalysed the oxidation of their substrates by a-ketonic acids. Some, like the triosephosphate mutase, also catalysed the dismutation of the substrate. Mutase action was inhibited almost completely by low concs. of iodoacetic acid. The coenzyme functioned in these oxidoreductions by undergoing a cycle of oxidation and reduction. Mutase systems did not react with O carriers such as flavin, methylene blue etc., in the absence of a thermolabile factor found in skeletal and cardiac muscle extracts. The factor was non-dialysable and was sedimented by high speed centrifuging; it was not identical with any of the known carriers. The reaction between lactate and phosphoglycerate yielding triosephosphate and pyruvate was shown to take place in presence of the triosephosphate mutase system and strong cyanide. The theory of mutase action was discussed.

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