Regulation of the activity of microbial kynureninase by transamination of the enzyme-bound coenzyme.
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.
D000409:Alanine; D006867:Hydrolases / Q000378:metabolism*; D007737:Kynurenine; D011485:Protein Binding; D011549:Pseudomonas / Q000201:enzymology*; D011732:Pyridoxal Phosphate; D011773:Pyruvates; D013053:Spectrophotometry; D000637:Transaminases / Q000378:metabolism*
D011773:Pyruvates; D007737:Kynurenine; D011732:Pyridoxal Phosphate; D000637:Transaminases; D006867:Hydrolases; D000409:Alanine