TY - JOUR T1 - Cysteine conjugate beta-lyase. JF - Molecular Pharmacology JO - Mol Pharmacol SP - 761 LP - 765 VL - 23 IS - 3 AU - J Stevens AU - W B Jakoby Y1 - 1983/05/01 UR - http://molpharm.aspetjournals.org/content/23/3/761.abstract N2 - Cysteine conjugate beta-lyase from rat liver, an enzyme participating in a shunt from mercapturic acid synthesis, has been purified and found to be active with a number of compounds that bear nonpolar leaving groups on the beta-carbon of an amino acid substrate. Pyridoxal phosphate is considered to be a participant in the reaction. In addition to aromatic thioethers of cysteine, the enzyme is also active with two aliphatic amino acid derivatives, S-1,2-dichlorovinyl-L-cysteine and beta-chloroalanine. Evidence is presented that catalysis results in "suicide" inhibition with a partition ratio of about 600 for each of the substrates. ER -