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Abstract d-Proline reductase contains covalently bound pyruvate, which is probably bonded to the protein through an amide linkage. Reduction of the pyruvate carbonyl group leads to loss of enzyme activity. It is postulated that the nitrogen atom of proline adds to the carbonyl group of pyruvate and that this interaction facilitates the reductive cleavage of the carbon-nitrogen bond of proline.
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Hodgins et al. (1967) studied this question.
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