|
type |
Journal Article |
authors |
Stevens, J.; Jakoby, W. B. |
title |
Cysteine conjugate beta-lyase |
journal |
Mol Pharmacol |
Activity |
4.4.1.13 |
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 |
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