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Glutamate dehydrogenase (NAD dependent)
Reference: GTD-211

Glutamate dehydrogenase (NAD dependent)

Glutamate dehydrogenase (NAD dependent) from Microorganism L-Glutamate + H2O + NADP+ ----> 2-Oxoglutarate + NH3 + NADPH + H+ L-Glutamate + H2O + NADP+ <---- 2-Oxoglutarate + NH3 + NADPH + H+
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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:NAD+ oxydoreductase (deaminating)
  • Appearance: White amorphous powder lyophilized
  • Activity: Grade II, 100 U/mg-solid or more
  • Contaminants: NAD oxidase < 1.0×10-2 %
  • Stability: Stable at - 20 °C for at least one year
  • Molecular weight: approx. 260,000
  • Isoelectric point: 5.6
  • Michaelis constants: 9.21×10-3 M (NH3), 4.80×10-3M (α-Ketoglutarate),
    5.89×10-4M(NAD＋) 7.8×10-5M (L-Glutamate), 1.29×10-4M (NADH)
  • Structure: 6 subunits per mol of enzyme
  • Inhibitors: Heavy metals, PCMB, IAA
  • Optimum pH: 7.5 - 8.0 (α-KG→L-Glu), 9.0 (L-Glu→α-KG)
  • Optimum temperature: 55 °C (α-KG→L-Glu), 50 °C (L-Glu→α-KG)
  • pH Stability: pH 5.0 - 10.0 (25 °C, 20hr)
  • Thermal stability: below 50 °C (pH 8.3 ,10min)
  • EC # 1.4.1.2
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