|
type |
Journal Article |
authors |
Soda, K.; Moriguchi, M.; Tanizawa, K. |
title |
Regulation of the activity of microbial kynureninase by transamination of the enzyme-bound coenzyme |
journal |
Acta Vitaminol Enzymol |
Activity |
3.7.1.3 |
ui |
78100151 |
year |
(1975) |
volume |
29 |
number |
1-6 |
pages |
335-8 |
| |
keywords |
Alanine |
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. |
last changed |
2002/11/12 16:17 |
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