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  • Title: Regulation of the activity of microbial kynureninase by transamination of the enzyme-bound coenzyme.
    Author: Soda K, Moriguchi M, Tanizawa K.
    Journal: Acta Vitaminol Enzymol; 1975; 29(1-6):335-8. PubMed ID: 1244119.
    Abstract:
    Kynureninase was purified to homogeneity from the extracts of Pseudomonas marginalis and Neurospora crassa. The active kynureninase containing pyridoxal 5'-phosphate transaminates with L-ornithine or L-alanine to form the inactive pyridoxamine 5'-phosphate form of enzyme and delta1-pyrroline-2-carboxylate or pyruvate. This inactive enzyme transaminates with pyruvate to restore the active pyridoxal 5'-phosphate enzyme and L-alanine. The activity of kynureninase is regulated in this manner by transamination of the coenzyme moiety.
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