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:
All
Chemical Reagents
Biomedicine
Organic raw materials
Inorganic chemical industry
intermediate
Agricultural chemicals
Auxiliaries and catalysts
Fragrances and Flavors
Dyes and Pigments
Daily chemical industry
重组亮氨酸脱氢酶 (LeuDH)
CAS number：unknown molecular formula：
overview
compound introduction
Specs
| Chinese alias | - | ||
| English alias | ldh | ||
| CAS number | unknown | molecular formula | |
| molecular weight | - | Exact mass | 生物活性 |
| PSA | - | logp | - |
numbering system
No numbering system information yet
physicochemical properties
No physical and chemical property information yet
Safety information
No safety information yet
Production methods and uses
No production method and use information yet
Related
upstream information
No upstream information yet
downstream information
No downstream information yet
MSDS
Found 0 shareMSDS
