Oxidative deamination of S-(1-carboxyethyl)-L-cysteine and S-(1-carboxypropyl)-L-cysteine by L-aminoacid oxidase.
S-(1-carboxyethyl)-L-cysteine (1-CEC) and S-(1-carboxypropyl)-L-cysteine (1-CPC) are oxidatively deaminated by L-aminoacid oxidase with consumption of half a mole of oxygen per mole of substrate in the presence of catalase. This reaction gives rise to the corresponding alpha-ketoacids, identified by some chemical and chromatographic tests and by comparison with synthetic compounds. It has been possible, therefore, to demonstrate that S-(1-carboxyethyl)-thiopvruvic acid (1-CETP) and S-(1-carboxypropyl)-thiopvruvic acid (1-CPTP) are the main products of oxidative deamination of 1-CEC and 1-CPC.
D000594:Amino Acid Oxidoreductases / Q000494:pharmacology*; D002233:Carbocysteine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D003545:Cysteine / Q000031:analogs & derivatives*; D003641:Deamination; D007700:Kinetics; D050830:L-Amino Acid Oxidase; D010100:Oxygen / Q000378:metabolism; D013379:Substrate Specificity; D013997:Time Factors
C052226:S-(1-carboxyethyl)cysteine; C052225:S-(1-carboxypropyl)cysteine; C018243:S-(2-carboxyethyl)cysteine; D002233:Carbocysteine; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase; D003545:Cysteine; D010100:Oxygen