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:
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