L-Leucine Dehydrogenase (Crude Enzyme)

L-leucine dehydrogenase (LeuDH), with the Enzyme Commission number EC 1.4.1.9, is an enzyme that catalyzes the oxidative deamination of L-leucine to α-ketoisocaproate and ammonia, using NAD⁺ as an electron acceptor. This reaction is reversible, allowing the enzyme to also catalyze the reductive amination of α-ketoisocaproate back to L-leucine. LeuDH plays a crucial role in nitrogen metabolism by contributing to the balance between amino acids and keto acids.

Alfa Chemistry offers high-quality L-leucine dehydrogenase that is briefly purified from engineered E. coli.

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Biological Significance

• Amino Acid Catabolism: LeuDH is crucial for the breakdown of leucine, an essential amino acid. This process regulates intracellular amino acid levels and provides alternative energy sources during periods of excess amino acids or limited glucose availability.
• Energy Production: LeuDH facilitates the conversion of leucine into intermediates that enter the citric acid cycle or gluconeogenesis, leading to ATP production and supporting cellular energy metabolism.
• Redox Homeostasis: The enzyme produces NADH during leucine catabolism, which helps maintain cellular redox balance by acting as a reducing agent in various metabolic reactions, including ATP synthesis.

Biotechnological Applications

Amino Acid Analysis

LeuDH is utilized in analytical techniques to quantify leucine and other amino acids in biological samples. Enzymatic analysis with LeuDH offers a specific and reliable method for detecting amino acids, making it invaluable in clinical diagnostics and research.

Synthesis of Chiral Compounds

The enzyme's ability to reversibly convert leucine to α-ketohexanoic acid is exploited in the production of chiral compounds. This capability is particularly valuable in synthesizing pharmaceutical intermediates, fine chemicals, and enantiopure amino acids, essential in drug development and other high-precision applications.

Metabolic Engineering

LeuDH is a tool in metabolic engineering strategies aimed at altering the metabolic flux of leucine and related amino acids. By manipulating this enzyme, scientists can enhance the production of specific amino acids or target the synthesis of desirable compounds derived from leucine catabolism. This approach holds promise for improving yields in biotechnological production processes.

Drug Discovery

Understanding the structure and function of LeuDH has significant implications for drug discovery. Modulators of this enzyme's activity could be developed as therapeutic agents for conditions related to leucine metabolism, such as maple syrup urine disease or other branched-chain amino acid disorders. This insight could lead to novel treatments and improved management of these diseases.

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