Oxidative deamination of S-aminopropylcysteine and S-aminoethylhomocysteine.
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.
Serao
I
I
Dipartimento di Scienze Biochimiche, Università La Sapienza, Roma, Italy.
Costa
M
M
Pecci
L
L
Coccia
R
R
Cavallini
D
D
D000588:Amines / Q000378:metabolism; D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000818:Animals; D002374:Catalase / Q000378:metabolism; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D003641:Deamination; D006710:Homocysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D007659:Ketones / Q000378:metabolism; D050830:L-Amino Acid Oxidase; D010084:Oxidation-Reduction; D012910:Snake Venoms / Q000201:enzymology*
D000588:Amines; D007659:Ketones; D012910:Snake Venoms; D006710:Homocysteine; C056572:aminopropylcysteine; C056573:5-(2-aminoethyl)homocysteine; D002374:Catalase; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase; D003545:Cysteine