The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination
نویسندگان
چکیده
منابع مشابه
The Mechanism of Glutamate Dehydrogenase Reaction IV. EVIDENCE FOR RANDOM AND RAPID BINDING OF SUBSTRATE AND COENZYME IN THE BURST
Stopped flow studies of the oxidative deamination of L-glutamate by TPN and beef liver glutamate dehydrogenase were performed at pH 6.5 and 7.6. At each pH value, the initial burst slopes obey an equation of the form: e/v = 40 + dd(TPN) + h/bglutamate) + &/(TPN)(L-glutamate). The agreement of dissociation constants for enzyme-TPN and enzyme-L-glutamate binary complexes obtained from the r#~ val...
متن کاملconsequence analysis of the leakage, ignition and explosion during high pressure sour gas injection process to the oil reservoir
there is no doubt that human being needs to become integrated with industry and industry needs to be progressed, daily. on the other hand, serious events in industrial units specially in oil industries has been shown that such damages and events are industry related ones. the consequence of such events and damages which resulted in chemical and poisoned explosions and loss of life and property ...
The mechanism of glutamate dehydrogenase reaction. IV. Evidence for random and rapid binding of substrate and coenzyme in the burst phase.
Stopped flow studies of the oxidative deamination of L-glutamate by TPN and beef liver glutamate dehydrogenase were performed at pH 6.5 and 7.6. At each pH value, the initial burst slopes obey an equation of the form: e/v = 40 + dd(TPN) + h/bglutamate) + &/(TPN)(L-glutamate). The agreement of dissociation constants for enzyme-TPN and enzyme-L-glutamate binary complexes obtained from the r#~ val...
متن کاملBinding studies of a spin-labelled oxidized coenzyme to bovine-liver glutamate dehydrogenase.
NAD+ with a nitroxide piperidine ring linked to the NH2 group of the adenine possesses full coenzymatic activity with glutamate dehydrogenase. Electron spin resonance spectra in the presence of glutamate dehydrogenase show mixtures of free and strongly immobilized spin-label. Binding studies in phosphate buffer demonstrate: (a) weak binary binding to the enzyme with a dissociation constant in t...
متن کاملSubstitutions at the cofactor phosphate-binding site of a clostridial alcohol dehydrogenase lead to unexpected changes in substrate specificity
Changing the cofactor specificity of an enzyme from nicotinamide adenine dinucleotide 2'-phosphate (NADPH) to the more abundant NADH is a common strategy for increasing overall enzyme efficiency in microbial metabolic engineering. The aim of this study was to switch the cofactor specificity of the primary-secondary alcohol dehydrogenase from Clostridium autoethanogenum, a bacterium with conside...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1993
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1993.tb17838.x