CAS 9082-71-7
:Leucine dehydrogenase
Description:
Leucine dehydrogenase is an enzyme that catalyzes the oxidative deamination of leucine, an essential amino acid, converting it into α-ketoisocaproate while reducing NAD+ to NADH. This enzyme plays a crucial role in amino acid metabolism and is involved in the regulation of nitrogen balance in organisms. Leucine dehydrogenase is typically found in various tissues, including the liver, and is important for energy production and metabolic pathways. The enzyme operates optimally at specific pH and temperature ranges, which can vary depending on the source organism. It is characterized by its specificity for leucine and its cofactor requirement, usually involving NAD+ or NADP+. The enzyme's activity can be influenced by various factors, including substrate concentration, pH, and the presence of inhibitors or activators. Due to its role in metabolism, leucine dehydrogenase is of interest in biochemical research and potential therapeutic applications, particularly in metabolic disorders.
Formula:Unspecified
Synonyms:- E.C. 1.4.1.9
- EC 1.4.1.9
- L-Leucine dehydrogenase
- Dehydrogenase, leucine
- Leucine dehydrogenase
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Found 4 products.
Leucine dehydrogenase
CAS:<p>Leucine dehydrogenase from Bacillus spheroides oxidizes/reduces branched-chain amino acids and their keto analogs.</p>Color and Shape:SolidL-Leucine dehydrogenase from bacillus cereus
CAS:<p>L-Leucine dehydrogenase (Leucine dehydrogenase, systematic name L-leucine:NAD+ oxidoreductase (deaminating); EC 1.4.1.9) is an enzyme that catalyzes the following reaction: L-leucine + H2O + NAD+ ⇌ 4-methyl-2-oxopentanoate + NH3 + NADH + H+ One unit of L-Leucine dehydrogenase will convert 1.0 µmole of L‑leucine into 4-methyl-2-oxopentanoate per min at pH 10.5 and 37 °C in the presence of NAD+. The enzyme requires NAD+ as a cofactor, it is available here.</p>Purity:Min. 95%
