Oxidative deamination of S-aminopropylcysteine and S-aminoethylhomocysteine

Ital J Biochem. 1991 Jul-Aug;40(4):216-22.

Abstract

S-aminopropylcysteine and S-aminoethylhomocysteine are oxidized by snake venom L-amino acid oxidase in the presence of catalase with formation of the respective ketoderivatives. Only the ketoderivative of S-aminopropylcysteine cyclizes to give a seven membered ring (ketimine) absorbing at 296 nm. In the absence of catalase both ketoderivatives are oxidatively decarboxylated.

MeSH terms

  • Amines / metabolism
  • Amino Acid Oxidoreductases / metabolism*
  • Animals
  • Catalase / metabolism
  • Cysteine / analogs & derivatives*
  • Cysteine / metabolism
  • Deamination
  • Homocysteine / analogs & derivatives*
  • Homocysteine / metabolism
  • Ketones / metabolism
  • L-Amino Acid Oxidase
  • Oxidation-Reduction
  • Snake Venoms / enzymology*

Substances

  • Amines
  • Ketones
  • Snake Venoms
  • Homocysteine
  • aminopropylcysteine
  • 5-(2-aminoethyl)homocysteine
  • Catalase
  • Amino Acid Oxidoreductases
  • L-Amino Acid Oxidase
  • Cysteine