|Related Categories||1.4.x.x Acting on CH-NH2, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index,|
|form||ammonium sulfate suspension|
|Gene Information||cow ... GLUD1(281785)|
Protein determined by biuret
One unit will reduce 1.0 μmole of α-ketoglutarate to
Suspension in 2.0 M (NH4)2SO4 solution, pH 7.0
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate<<<24,25>>
Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes.
The bovine enzyme is characterized by three sets of properties:
• It has a reversible concentration-dependent association, producing higher molecular weight forms.
• Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.
• Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
Customers Also Viewed
sufficient for 100 assays
buffered aqueous solution, ≥400 units/mg protein (biuret)
Type II, buffered aqueous glycerol solution, ≥35 units/mg protein
Type III, lyophilized powder, ≥20 units/mg protein
Certificate of Analysis
Certificate of Origin
Note that for an ammonium sulfate suspension, most of the enzyme will be in solid form. It is likely that only negligible amounts of enzyme will be in the ammonium sulfate solution.
Keywords: Enzyme activity
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Enhancing the flux of D-glucose to the pentose phosphate pathway in Saccharomyces cerevisiae for the production of D-ribose and ribitol. Toivari MH, Maaheimo H, Penttilä M, et al. Appl. Microbiol. Biotechnol. 85(3), 731-9, (2010)
A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis. Bailey J, Powell L, Sinanan L, et al. FEBS J. 278(17), 3140-51, (2011)
Biochemical evaluation of an infant with hypoglycemia resulting from a novel de novo mutation of the GLUD1 gene and hyperinsulinism-hyperammonemia syndrome. Balasubramaniam S, Kapoor R, Yeow JH, et al. J. Pediatr. Endocrinol. Metab. 24(7-8), 573-7, (2011)
Overexpression in a non-native halophilic host and biotechnological potential of NAD+-dependent glutamate dehydrogenase from Halobacterium salinarum strain NRC-36014. Munawar N and Engel PC Extremophiles 16(3), 463-76, (2012)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?