Leucine dehydrogenase, Microorganism  (Synonyms: LDH, EC 1.4.1.9)

Leucine dehydrogenase, Microorganism (EC 1.4.1.9) can be purified from Bacillus spheroides. Leucine dehydrogenase catalyzed the oxidative deamination of L-leucine, L-valine, L-isoleucine, L-norvaline, L-alpha-aminobutyrate, and L-norleucine, and the reductive amination of their keto analogues^[1].

Product Information
Molecular weight: 43 kDa (SDS-PAGE)
Isoelectric point: 6.6
Km value: 2.6×10^-4 M (NAD ), 2.0×10^-3 M(L-Leucine) , 6.8×10^-4 M(α-Ketoisocaproate), 4.2×10^-2 M (NH Cl), 2.3×10^-4 M (NADH)
pH stability: 6.0-11.0 (25°C, 15 hr)
Optimum temperature: 55-60°C
Inhibitor: Hg²⁺

Instructions
Dissolved in water (1 mg/mL), or in buffer according to the specific experimental reference.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9082-71-7

Solid

White to light yellow

[Leucine dehydrogenase, Microorganism]

1.4.1.9

≥25 U/mg protein

One unit is defined as the amount of enzyme that will convert 1.0 μmole of L-leucine to αketoisocaproate per min at pH 10.5 at 37°C.

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Ohshima T, et al. Properties of crystalline leucine dehydrogenase from Bacillus sphaericus. J Biol Chem. 1978 Aug 25;253(16):5719-25.  [Content Brief]