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B6db references: 83244517

type Journal Article
authors Stevens, J.; Jakoby, W. B.
title Cysteine conjugate beta-lyase
journal Mol Pharmacol
ui 83244517
year (1983)
volume 23
number 3
pages 761-5.
keywords Animal
abstract 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.
last changed 2002/11/12 16:17

B6db references