The use of multiwavelength kinetic analysis approach to identify and characterize intermediate complexes in the reductive amination reaction catalyzed by bovine liver glutamate dehydrogenase-Reference-Cited by-同舟云学术

The use of multiwavelength kinetic analysis approach to identify and characterize intermediate complexes in the reductive amination reaction catalyzed by bovine liver glutamate dehydrogenase

Published:1998-01 Issue:1 Volume:1382 Page:8-12
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Saha Swapan K.,Maniscalco Steven J.,Fisher Harvey F.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference6 articles.

1. Thermodynamics of the glutamate dehydrogenase catalytic reaction

2. The real-time resolution of proton-related transient-state steps in an enzymatic reaction. The early steps in the oxidative deamination reaction of bovine liver glutamate dehydrogenase.

3. Beef liver L-glutamate dehydrogenase mechanism: Presteady state study of the catalytic reduction of 2.oxoglutarate by NADPH

4. Ultraviolet Spectrophotometric Characterization of a Glutamate Dehydrogenase-reduced Coenzyme-α-Ketoglutarate Complex

5. The demonstration of a glutamate dehydrogenase-NADP-L-glutamate charge-transfer complex and its location on the reaction pathway.

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2. The interpretation of multiple-step transient-state kinetic isotope effects;Archives of Biochemistry and Biophysics;2004-05

3. Identification and Characterization of Kinetically Competent Carbinolamine and α-Iminoglutarate Complexes in the Glutamate Dehydrogenase-Catalyzed Oxidation of l-Glutamate Using a Multiwavelength Transient State Approach;Biochemistry;1998-09-26