Steady-state kinetics and transient studies of substrate and coenzyme analogue binding to clostridial glutamate dehydrogenase (GDH) during oxidative deamination.
Basso
L A
LA
Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
Engel
P C
PC
Walmsley
A R
AR
D001665:Binding Sites; D003013:Clostridium / Q000201:enzymology*; D003067:Coenzymes / Q000378:metabolism; D003641:Deamination; D005969:Glutamate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D018698:Glutamic Acid / Q000378:metabolism; D007700:Kinetics; D009243:NAD / Q000031:analogs & derivatives / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
D003067:Coenzymes; D009243:NAD; C011038:nicotinamide 1,N(6)-ethenoadenine dinucleotide; D018698:Glutamic Acid; D005969:Glutamate Dehydrogenase