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Wichtige Dokumente
G4387
L-Glutamic Dehydrogenase (NADP) from Proteus sp.
buffered aqueous solution, ≥4,000 units/mL
Synonym(e):
L-Glutamate:NADP+ oxidoreductase (deaminating)
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Alle Fotos(6)
About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
Biologische Quelle
bacterial (Proteus spp.)
Qualitätsniveau
Form
buffered aqueous solution
Spezifische Aktivität
≥4,000 units/mL
Mol-Gew.
~300 kDa
Lagertemp.
2-8°C
Anwendung
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 L-glutamate, in the presence of excess ammonium ions (NH4+) and NADPH.
Biochem./physiol. Wirkung
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
Physikalische Eigenschaften
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)
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)
Einheitendefinition
One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30 °C in the presence of ammonium ions and NADPH.
Physikalische Form
Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide
Sonstige Hinweise
Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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D P Hornby et al.
The Biochemical journal, 223(1), 161-168 (1984-10-01)
In steady-state kinetic studies of ox liver glutamate dehydrogenase in 0.11 M-potassium phosphate buffer, pH7, at 25 degrees C, the concentration of ADP was varied from 0.5 to 1000 microM. Inhibition was observed except when the concentrations of both glutamate
J Bailey et al.
The Journal of biological chemistry, 257(10), 5579-5583 (1982-05-25)
The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At ph 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both
Marta Rodríguez-Sáiz et al.
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The gdhA gene encoding the NADP-dependent glutamate dehydrogenase (GDH) activity from Xanthophyllomyces dendrorhous has been cloned and characterized, and its promoter used for controlled gene expression in this red-pigmented heterobasidiomycetous yeast. We determined the nucleotide sequence of a 4701 bp
Tom A Williams et al.
Molecular biology and evolution, 26(2), 445-450 (2008-11-28)
Aminoacyl tRNA synthetases (aaRS) are crucial enzymes that join amino acids to their cognate tRNAs, thereby implementing the genetic code. These enzymes fall into two unrelated structural classes whose evolution has not been explained. The leading hypothesis, proposed by Rodin
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