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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

Catalog Number PKG Qty. Price Quantity
45-G4387-1KU 1000 units
$225.00
1/EA
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45-G4387-5KU 5000 units
$779.00
1/EA
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Figure 1. Stability (solution); 50% glycerol solution in 25 mM Tris-HCl buffer containing 2.5 mM EDTA, pH 7.8.
Figure 2. Stability (suspension); 3.0 M ammonium sulfate suspension in 50 mM Tris-HCl buffer containing 5 mM EDTA. pH 7.8
Figure 3. Initial activity of the enzyme as a function of the pH of the assay reaction
Figure 4. Initial activity of the enzyme as a function of the temperature of the assay reaction
Figure 5. pH Stability; 25 °C, 20-hr treatment with 0.1 M buffer solution: pH 4.4–6.2, acetate; pH 6.2–8.4, phosphate; pH 8.8–10.2, glycine-NaOH
Figure 6. Thermal stability; 10-min. treatment with 0.1 M K-phosphate buffer, pH 7.4

 

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 L-glutamate, in the presence of excess ammonium ions (NH4+) and NADPH.
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 L-GLDH, EC 1.4.1.3.
Other Notes: 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.
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  | IUBMB  )
UNSPSC 12352204

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