Journal article
Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes
Molecular pharmacology, Vol.21(2), pp.444-448
01/01/1982
DOI: 10.1016/S0026-895X(25)14616-6
PMID: 6892478
Abstract
An acetyltransferase from rat kidney microsomes that catalyzes the N-acetylation of thioethers of L-cysteine has been solubilized, stabilized, and separated from hydrolytic enzymes active against both the acetylated product, a mercapturic acid, and acetyl coenzyme A. Efficiency of catalysis varies with the lipophilicity of the substituent at sulfur in the order, ethyl < propyl < benzyl < butyl, as predicted by the Hansch pi constants. Although L-tryptophan is acetylated at a very low rate, acetylation is not detectable for L-cysteine, L-methionine, L-serine, L-leucine, L-phenylalanine, or L-glutamic acid. The properties and substrate specificity reported here, along with previous studies on enzyme distribution, suggest that cysteine S-conjugate N-acetyltransferase is responsible for the final step in mercapturic acid biosynthesis.
Details
- Title: Subtitle
- Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes
- Creators
- Michael W DuffelWilliam B Jakoby
- Resource Type
- Journal article
- Publication Details
- Molecular pharmacology, Vol.21(2), pp.444-448
- DOI
- 10.1016/S0026-895X(25)14616-6
- PMID
- 6892478
- ISSN
- 0026-895X
- eISSN
- 1521-0111
- Language
- English
- Date published
- 01/01/1982
- Academic Unit
- Pharmaceutical Sciences and Experimental Therapeutics; Medicinal and Natural Products Chemistry
- Record Identifier
- 9984303163002771
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