Enzyme involved in amino acid metabolism

Enzymes involved in amino acid metabolism refer to a diverse group of proteins catalyzing the synthesis, breakdown, and interconversion of amino acids within living organisms. These enzymes are classified into several major types, including aminotransferases (which mediate transamination), deaminases (which remove amino groups), synthetases (which join amino acids with other substrates), and hydrolases (which catalyze hydrolysis of peptide bonds and other substrates). Notable examples include asparaginase, arginase, glutaminase, tryptophan dioxygenase, and indoleamine 2,3-dioxygenase. Dysfunction of these enzymes or their dysregulation is closely linked to various diseases, including cancers (where tumors exploit or become dependent on particular amino acid metabolic pathways), metabolic and cardiovascular diseases, and immune abnormalities. Many enzymes in amino acid metabolism are considered valid or emerging therapeutic targets because their activity is essential for tumor survival, immune evasion, or progression of metabolic diseases. Drugs targeting these enzymes mostly act via competitive or allosteric inhibition, substrate depletion, or immunomodulation, but therapeutic use can be limited by specificity, adaptive resistance, and safety issues such as immunosuppression or off-target effects[2][3][6][9][10].

Other names

Amino acid-metabolizing enzymeEnzyme of amino acid metabolic pathwayAminotransferase (subtype)Transaminase (subtype)Deaminase (subtype)Asparaginase (specific subtype)Arginase (specific subtype)Glutaminase (specific subtype)

Enzyme inhibition (e.g., blocking catalytic activity), Substrate depletion (e.g., serum amino acid depletion), Immunomodulation (e.g., altering immune cell metabolism), Induction of metabolic stress in target cells