Lysine—pyruvate 6-transaminase

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Lysine—pyruvate 6-transaminase is an enzyme that catalyzes the chemical reaction between L-lysine and pyruvate, facilitating the transfer of an amino group from L-lysine to pyruvate, resulting in the production of L-glutamate and alpha-aminoadipate. This enzyme plays a crucial role in the metabolic pathways of amino acid metabolism, specifically in the degradation and synthesis of amino acids, which are vital for various biological processes including protein synthesis, energy production, and neurotransmitter regulation.

Function[edit | edit source]

Lysine—pyruvate 6-transaminase is involved in the catabolism of L-lysine, an essential amino acid that must be obtained through the diet as it cannot be synthesized by the human body. This enzyme's activity is essential for the conversion of L-lysine into metabolites that can enter the Krebs cycle (also known as the citric acid cycle or TCA cycle), a critical step in cellular respiration and energy production. By transferring an amino group from L-lysine to pyruvate, it forms L-glutamate and alpha-aminoadipate, intermediates in the metabolic pathway that leads to the production of energy and the synthesis of other amino acids.

Mechanism[edit | edit source]

The mechanism of action of lysine—pyruvate 6-transaminase involves the transfer of an amino group from L-lysine, a basic amino acid, to pyruvate, a key intermediate in several metabolic pathways. This transamination process is facilitated by the presence of a coenzyme, typically pyridoxal phosphate (PLP), which acts as a carrier for the amino group during the reaction. The enzyme-substrate complex undergoes a series of conformational changes, leading to the transfer of the amino group and the release of the products, L-glutamate, and alpha-aminoadipate.

Clinical Significance[edit | edit source]

Alterations in the activity of lysine—pyruvate 6-transaminase can have significant clinical implications. Deficiencies in this enzyme can lead to metabolic disorders characterized by abnormal levels of lysine and its metabolites in the body. Such conditions can result in neurological issues, growth retardation, and other metabolic complications. Understanding the function and regulation of this enzyme is crucial for the development of therapeutic strategies for treating metabolic disorders related to amino acid metabolism.

See Also[edit | edit source]

References[edit | edit source]


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Contributors: Prab R. Tumpati, MD