Sorachim
Reference: GTD-209

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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  • This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201, URH-301) in clinical analysis.
  • Product name: L-Glutamate:NADP+ oxydoreductase (deaminating)
  • Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and
  • 5.0mM EDTA, pH 7.8
  • Activity: Grade II 300U/mg-protein or more
  • Contaminants: NADPH oxidase < 1.0×10-2%
  • Glutathione reductase < 1.0×10-2%
  • Stability Stable at 5 °C for at least 6 months
  • Molecular weight approx. 300,000
  • Isoelectric point 4.6
  • Michaelis constants 1.1×10-3 M (NH3), 3.4×10-4M (α-Ketoglutarate)
  • 1.2×10-3M (L-Glutamate), 1.4×10-5M (NADPH), 1.5×10-5M (NADP+)
  • Structure 6 subunits (M.W.50,000) per mol of enzyme
  • Inhibitors Hg2+ , Cd2+, 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 45 °C (α-KG→L-Glu) 45 - 55 °C (L-Glu→α-KG)
  • pH stability pH 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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