The use of multiwavelength kinetic analysis approach to identify and characterize intermediate complexes in the reductive amination reaction catalyzed by bovine liver glutamate dehydrogenase.
A multiwavelength transient-state kinetic study of the glutamate dehydrogenase catalyzed reaction has proven that an alpha-iminoglutarate complex is an observable intermediate in the reverse direction. It also shows the existence of two enzyme-NADPH-ketoglutarate complexes, only one of which reacts with ammonia rapidly.
Saha
S K
SK
Laboratory of Molecular Biochemistry, Veterans Affairs Medical Center, Kansas City, MO, USA.
Maniscalco
S J
SJ
Fisher
H F
HF
D000818:Animals; D002417:Cattle; D005969:Glutamate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007097:Imines; D007656:Ketoglutaric Acids; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet
D007097:Imines; D007656:Ketoglutaric Acids; D009249:NADP; D005969:Glutamate Dehydrogenase