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Pyridoxal 5'-phosphate-dependent aminotransferases are a large family of enzymes that catalyze the transfer of amino groups between amino acids and keto acids, a central function in amino acid metabolism. Their activity depends on the cofactor pyridoxal 5'-phosphate (PLP), which acts as an electron sink and forms a Schiff base with amino acid substrates. These enzymes are widespread, essential for nitrogen metabolism, and structurally classified into distinct evolutionary families. Their malfunction is clinically relevant in liver disease, metabolic defects, and vitamin B6 deficiency syndromes
Aminotransferases catalyze the reversible transfer of an amino group from an amino acid to a keto acid using PLP as a coenzyme, relying on formation of external and internal aldimines and electron sink chemistry
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