L-glutamate dehydrogenase (GDH) (EC 1.4.1.2) is a crucial enzyme in cellular metabolism that plays a significant role in the deamination of the amino acid glutamate. This enzyme is typically hexameric, consisting of six identical subunits, each housing an active site where the reaction occurs. GDH requires the cofactors NAD+ (nicotinamide adenine dinucleotide) or NADP+ (nicotinamide adenine dinucleotide phosphate) to function effectively. It catalyzes the reversible oxidative deamination of L-glutamate into α-ketoglutarate and ammonia, thereby facilitating important metabolic processes within the cell.
Alfa Chemistry offers high-quality L-glutamate dehydrogenase that is briefly purified from engineered E. coli.
Product Detail
Product Name | L-Glutamate Dehydrogenase (Crude Enzyme) |
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Catalog Number | BIOS9001461 |
CAS Number | 9001-46-1 |
Enzyme Commission Number | EC 1.4.1.2 |
Source | E. coli |
Enzymatic Reaction | L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+ |
Synonyms | Glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase |
Systematic Name | L-glutamate:NAD+ oxidoreductase (deaminating) |
Cofactor(s) | NAD+; NADH; NADP+; NADPH |
Applications | Biotechnology; diagnostics; medicine; analysis; agriculture |
Storage | Store at -20 °C or lower, for at least 1 month. |
Biological Role and Functions
- Amino Acid Metabolism: GDH is crucial in amino acid catabolism, specifically in the degradation of glutamate, which can then feed into the Krebs (TCA) cycle as α-ketoglutarate, a key metabolic intermediate.
- Nitrogen Metabolism: It plays a role in nitrogen metabolism by regulating the levels of ammonia and glutamate in cells.
- Energy Production: By converting glutamate into α-ketoglutarate, GDH links amino acid metabolism with the TCA cycle, thus playing a part in cellular energy production.
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