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Key Documents

G4387

Sigma-Aldrich

L-Glutamic Dehydrogenase (NADP) from Proteus sp.

buffered aqueous solution, ≥4,000 units/mL

Sinonimo/i:

L-Glutamate:NADP+ oxidoreductase (deaminating)

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

bacterial (Proteus spp.)

Livello qualitativo

Forma fisica

buffered aqueous solution

Attività specifica

≥4,000 units/mL

PM

~300 kDa

Temperatura di conservazione

2-8°C

Applicazioni

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.

Azioni biochim/fisiol

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.

Proprietà fisiche

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)

Definizione di unità

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.

Stato fisico

Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide

Altre note

Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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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
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
Daria V Borsakova et al.
Scientific reports, 12(1), 5437-5437 (2022-04-02)
Excessive ammonium blood concentration causes many serious neurological complications. The medications currently used are not very effective. To remove ammonium from the blood, erythrocyte-bioreactors containing enzymes that processing ammonium have been proposed. The most promising bioreactor contained co-encapsulated glutamate dehydrogenase
Tomomi Abiko et al.
Planta, 232(2), 299-311 (2010-05-06)
In plants, glutamine synthetase (GS) is the enzyme that is mainly responsible for the assimilation of ammonium. Conversely, in microorganisms such as bacteria and Ascomycota, NADP(H)-dependent glutamate dehydrogenase (GDH) and GS both have important roles in ammonium assimilation. Here, we
Daniel Juan Herrera et al.
Annals of clinical biochemistry, 47(Pt 1), 81-83 (2009-11-27)
Enzymatic assays using glutamate dehydrogenase (GLDH) to monitor the transformation of NAD(P)H to NAD(P)(+) by a spectrophotometric technique are the most common methods to measure plasma ammonia (PA) in routine laboratories worldwide. However, these assays can potentially be subject to

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