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Glutamate dehydrogenase (NADP dependent)
Reference: GTD-409

Glutamate dehydrogenase (NADP dependent)

Glutamate dehydrogenase (NADP dependent) from Proteus sp. L-Glutamate + H2O + NADP+ ----> 2-Oxoglutarate + NH3 + NADPH + H+ L-Glutamate + H2O + NADP+ <---- 2-Oxoglutarate + NH3 + NADPH + H+ This enzyme is used for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease.
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DESCRIPTION
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  • Product name: L-Glutamate:NADP+ oxydoreductase (deaminating)
  • Appearance: 50mM Tris buffer solution at pH 7.8 with 0.05% NaN3 and 5mM EDTA
  • Activity: > 9000 U/ml
  • Contaminants: NADPH oxidase ≤ 0.01 %, Gluthathione reductase ≤ 0.01 %
  • Stabilizer: EDTA
  • Stability: Stable at 2-8°C for at least 6 months
  • Molecular weight: Approx. 300,000
  • Isoelectric point: 4.6
  • Michaelis constants: 1.1×10-3 M (NH3), 3.4×10-4 M (α-Ketoglutarate), 1.5x10-5M (NADP+)
    1.2×10-3 M (L-Glutamate), 1.4x10-5M (NADPH)
  • Structure: 6 subunits per mol of enzyme
  • Inhibitors: Heavy metals, PCMB, Pyridine, 4-4’-dithiopyridine, 2-2’-dithiopyridine
  • Optimum pH: 8.5 (α-KG ->L-Glu), 9.8 (L-Glu ->α-KG)
  • Optimum temperature: 45°C (α-KG ->L-Glu), 45-55°C (L-Glu ->α-KG)
  • pH stability: 6.0 – 8.5 (25°C, 20hr)
  • Thermal stability: Below 50°C (pH 7.4, 10min)
  • EC # 1.4.1.4
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