| Cat# | NATE-1715 |
| Abbr | LEDH (Microorganism) |
| Source | Microorganism |
| Description | In enzymology, a leucine dehydrogenase (EC 1.4.1.9) is an enzyme that catalyzes the chemical reaction: L-leucine + H2O + NAD+ ↔ 4-methyl-2-oxopentanoate + NH3 + NADH + H+. The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. |
| Form | White powder, lyophilized |
| Enzyme Commission Number | EC 1.4.1.9 |
| Activity | >500U/mg protein |
| CAS No. | 9082-71-7 |
| Molecular Weight | 43 kDa (SDS-PAGE) |
| Isoelectric point | 6.6 |
| pH Stability | 6.0~11.0 (25℃, 15hr) |
| 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 (NH Cl) 2.3×10^-4 M (NADH) |
| Unit Definition | One unit will convert one micromole of L-Leucine to α-Ketoisocaproate per minute at pH 10.5 at 37℃. |
| Optimum pH | above11.0(L-Leu→α-K I C), 8.5(α-K I C→L-Leu) |
| Optimum temperature | 55-60℃(L-Leu →α-K I C) above 60℃(α-K I C→L-Leu) |
| Thermal stability | < 55℃(pH 7.0, 20min) |
| Storage | Store at -20°C. |
| Inhibitors | Hg2+ |
| Synonyms | EC 1.4.1.9; Leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); L-leucine dehydrogenase; L-leucine: NAD+ oxidoreductase (deaminating); LeuDH |
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