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lysine carboxypeptidase [EC 3.4.17.3] an enzyme of the hydrolase class that catalyzes the removal of C-terminal basic amino acids from peptides, preferentially removing lysine residues but also removing arginine residues from kinins, inactivating them. The enzyme is found in plasma. Called also arginine carboxypeptidase and kininase I.
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lysine dehydrogenase an enzyme of the oxidoreductase class that catalyzes the oxidative deamination of lysine, removing the α-amino acid as the first step in a minor pathway of lysine degradation (see also α-aminoadipic semialdehyde synthase). Deficiency of the enzyme, an autosomal recessive trait, causes congenital lysine intolerance.
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lysine i., congenital an autosomal recessive disorder due to a defect in the degradation of lysine, characterized by high levels of ammonia, lysine, and arginine in the blood, with vomiting, rigidity, and coma. Cf. hyperlysinemia.
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lysine ketoglutarate reductase saccharopine dehydrogenase (NADP+, L-lysine-forming).
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lysine v. the antidiuretic hormone of the pig family, differing from arginine vasopressin in having lysine instead of arginine at position 8; used pharmaceutically as the synthetic preparation lypressin (q.v.).
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