L-Glutamic Dehydrogenase (NADP) from Proteus sp.
SIGMA/G4387 - buffered aqueous solution, ≥4,000 units/mL
Synonym: L-Glutamate:NADP+ oxidoreductase (deaminating)
CAS Number: 9029-11-2
MDL Number: MFCD00131461
Product Type: Chemical
| biological source | bacterial (Proteus spp.) |
| form | buffered aqueous solution |
| mol wt | ~300 kDa |
| Quality Level | 200 ![]() |
| specific activity | ≥4,000 units/mL |
| storage temp. | 2-8°C |
| Application: | This enzyme is useful for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201) in clinical analysis. In vitro, various activity assays of this enzyme examine the conversion of α-ketoglutarate to |
| Biochem/physiol Actions: | L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. |
| General description: | Isoelectric point : 4.6 Michaelis constants : 1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate) 1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+) Structure : 6 subunits (M.W.50,000) per mol of enzyme Inhibitors : Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine, 2,2′-dithiopyridine Optimum pH : 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG) Optimum temperature : 45oC(α-KG−L-Glu) 45-55oC (L-Glu→α-KG) pH stability : pH 6.0 - 8.5 (25oC, 20hr) Thermal stability : below 50oC (pH 7.4, 10min) |
| Other Notes: | Note: Do not confuse with non-specific |
| Other Notes: | One unit will reduce 1.0 μmole of α-ketoglutarate to |
| Physical form: | Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥4,000 units/mL |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 1.4.1.4 ( BRENDA ![]() ![]() |
| UNSPSC | 12352204 |

