重组亮氨酸脱氢酶 (LeuDH)

ldh

L774077-100U

100U

生物活性

≥80%(SDS-PAGE)

Leucine Dehydrogenase (LeuDH, EC 1.4.1.9) belongs to the oxidoreductase family and can highly specifically catalyze the oxidative deamination of branched-chain amino acids such as L-leucine. Using NAD⁺ as an essential cofactor, this enzyme reversibly catalyzes the oxidative deamination of L-leucine to produce α-ketoisocaproic acid (α-KIC) and ammonia (NH₃), while reducing NAD⁺ to NADH. Reaction Properties Source: Microorganism Isoelectric point: 6.6 Michaelis constant: 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 (NH3), 2.3×10^-4 M (NADH) Optimum pH: 11.0 (L-Leu→α-K I C), 8.5(α-K I C→ L-Leu) Fig. 1 Optimum temperature: 50-60℃ (L-Leu →α-K I C), 60~70℃ (α-K I C→ L-Leu) Fig. 3 pH Stability: 6.0~11.0 (25℃, 15hr) Fig. 2 Thermal stability:

≥25U/mg protein; Unit definition: One unit will convert one micromole of L-Leucine to αKetoisocaproate per minute at pH 10.5 at 37 ℃.

重组表达

43 kDa (SDS-PAGE)

E. coli Accession #: P0A393 | E. coli