Summary: Extracts of contain NADP-linked hydroxypyruvate reductase activity. The enzyme responsible has been separated and partially purified. It showed some activity with glyoxylate, acetoin, diacetyl and oxaloacetate and was 2 1/2 times as active with NADP as with NAD. It appears to be a constitutive enzyme and possible metabolic roles for it are discussed. Attention is drawn to the dangers of relying solely on the presence of hydroxypyruvate reductase as a diagnostic marker for the operation of a serine pathway of C-assimilation in a micro-organism. The malate dehydrogenase from has been partially purified and shown to possess no glycerate dehydrogenase or hydroxypyruvate reductase activity.


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