G4387

L-Glutamic Dehydrogenase (NADP) from Proteus sp.

buffered aqueous solution, ≥4,000 units/mL

• 동의어(들): L-Glutamate:NADP⁺ oxidoreductase (deaminating)
• CAS Number: 9029-11-2
• EC 번호: 1.4.1.4 (BRENDA, IUBMB)
• MDL number: MFCD00131461
• UNSPSC 코드: 12352204
• NACRES: NA.54

속성

• 생물학적 소스: bacterial (Proteus spp.)
• Quality Level: 200
• 양식: buffered aqueous solution
• 특이 활성도: ≥4,000 units/mL
• 분자량: ~300 kDa
• 저장 온도: 2-8°C

설명

애플리케이션

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.

생화학적/생리학적 작용

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.

물리적 특성

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 : 45^oC(α-KG−L-Glu) 45-55^oC (L-Glu→α-KG)
pH stability : pH 6.0 - 8.5 (25^oC, 20hr)
Thermal stability : below 50^oC (pH 7.4, 10min)

단위 정의

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.

물리적 형태

Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na₂EDTA containing 0.05% sodium azide

기타 정보

Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.

안전성 정보

• Storage Class Code: 10 - Combustible liquids
• WGK: WGK 3
• Flash Point (°F): Not applicable
• Flash Point (°C): Not applicable