Application This enzyme is useful for enzymatic determination of NH 3 , 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 (NH 4+ ) and NADPH. physical property Isoelectric point : 4.6 Michaelis constants : 1.1 X 10 -3 M (NH 3 ), 3.4 X 10 -4 M (α-Ketoglutarate) 1.2 X 10 -3 M (L-Glutamate), 1.4 X 10 -5 M (NADPH), 1.5 X 10 -5 M (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 : 45 o C(α-KG−L-Glu) 45-55 o C (L-Glu→α-KG) pH stability : pH 6.0 - 8.5 (25 o C, 20hr) Thermal stability : below 50 o C (pH 7.4, 10min)
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L-谷氨酸脱氢酶(NADP型)
CAS number:unknown molecular formula:
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compound introduction
Specs
| Chinese alias | - | ||
| English alias | L-Glutamate:NADP+ oxidoreductase (deaminating) | ||
| CAS number | unknown | molecular formula | |
| molecular weight | - | Exact mass | - |
| PSA | - | logp | - |
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