Abstract
Glyceraldehyde-3-phosphate dehydrogenases from mammalian muscle and yeast are known to display negative and positive cooperativity, respectively, in the binding of coenzyme, NAD. A possible physiological role of these coenzyme-binding anomalies is raised by comparing them to the coenzyme-binding properties of lactate dehydrogenase and alcohol dehydrogenase, the corresponding glycolytic NADH-reoxidizing enzymes in muscle and yeast. It is suggested that the observed coenzyme-binding relations reflect the evolutionary adaptation of enzymes to facilitate vectorial metabolite flow.
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