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Cysteine conjugate beta-lyase

J Stevens and WB Jakoby

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.

Volume 23, Issue 3, pp. 761-765, 05/01/1983
Copyright © 1983 by American Society for Pharmacology and Experimental Therapeutics




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Copyright © 1983 by the American Society for Pharmacology and Experimental Therapeutics