Mechanism of formation of bound alpha-iminoglutarate from alpha-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition.-Reference-Cited by-同舟云学术

Mechanism of formation of bound alpha-iminoglutarate from alpha-ketoglutarate in the glutamate dehydrogenase reaction. A chemical basis for ammonia recognition.

Published:1988-02 Issue:5 Volume:263 Page:2304-2308
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Srinivasan R,Viswanathan T S,Fisher H F

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference22 articles.

1. Effect of ammonia on the glutamate dehydrogenase catalyzed oxidative deamination of L-glutamate: production of an ammonia-containing intermediate in the "burst" phase

2. Glutamate dehydrogenase catalyzes the reduction of a Schiff base (delta 1-pyrroline-2-carboxylic acid) by NADPH.

3. Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH.

4. Catalysis of α-Iminoglutarate Formation from α-Ketoglutarate and Ammonia by Bovine Glutamate Dehydrogenase

5. Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphate

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