CYSTEINE CONJUGATE BETA-LYASE
- 1 January 1983
- journal article
- research article
- Vol. 23 (3) , 761-765
Abstract
Cysteine conjugate .beta.-lyase from rat liver, an enzyme participating in a shunt from mercapturic acid synthesis, was purified and was active with a number of compounds that bear nonpolar leaving groups on the .beta.-carbon of an amino acid substrate. Pyridoxal phosphate is a participant in the reaction. In addition to aromatic thioethers of Cys, the enzyme is also active with 2 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.This publication has 13 references indexed in Scilit:
- Thiol S-methyltransferase from rat liverArchives of Biochemistry and Biophysics, 1979
- Studies on the origin of the methylsulfonyl‐containing metabolites from propachlorJournal of Environmental Science and Health, Part B, 1979
- Cysteine conjugate beta-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs.Journal of Biological Chemistry, 1978
- Suicide substrates for the alanine racemase of Escherichia coli BBiochemistry, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A New Metabolic Pathway of Bromazepam Involving Attachment of a Methylthio GroupXenobiotica, 1975
- Cleavage of S-(1,2-dichlorovinyl)-l-cysteine by an enzyme of bovine originArchives of Biochemistry and Biophysics, 1965
- The biotransformation of a sulfonamide to a mercaptan and to mercapturic acid and glucuronide conjugatesBiochemical Pharmacology, 1965
- Interaction of S-(1,2-dichlorovinyl)-l-cysteine with proteinsArchives of Biochemistry and Biophysics, 1965
- Enzymic methylation of foreign sulfhydryl compoundsBiochimica et Biophysica Acta, 1961