Novel sources of mammalian C-S lyase activity

Adcock, H.J., Gaskin, P.J., Shaw, P.N., Teesdale-Spittle, P.H. and Buckberry, L.D. (1996) Novel sources of mammalian C-S lyase activity. Journal of Pharmacy and Pharmacology, 48 2: 150-153.

Author Adcock, H.J.
Gaskin, P.J.
Shaw, P.N.
Teesdale-Spittle, P.H.
Buckberry, L.D.
Title Novel sources of mammalian C-S lyase activity
Journal name Journal of Pharmacy and Pharmacology   Check publisher's open access policy
ISSN 0022-3573
Publication date 1996-02
Sub-type Article (original research)
Volume 48
Issue 2
Start page 150
End page 153
Total pages 4
Place of publication West Sussex, United Kingdom
Publisher John Wiley & Sons
Language eng
Formatted abstract
The C-S lysis of L-cysteine conjugates is one biotransformation pathway which is responsible for the generation of mutagenic and cytotoxic metabolic species. Thirteen cysteine S-conjugates were synthesized in our laboratories and incubated with aspartate aminotransferase (ASAT) and alanine aminotransferase (ALAT) enzymes from porcine heart tissue. The C-S lyase (CSL) activity for each enzyme-substrate combination was determined.

ASAT and ALAT were shown to exhibit CSL activity and it was also demonstrated that this activity was inhibited in the presence of the pyridoxal phosphate-dependent enzyme inhibitor amino(oxyacetic acid) confirming the pyridoxal phosphate-dependent mechanism by which C-S lysis is known to take place. This finding has potentially important implications for the risk assessment of compounds which produce L-cysteine conjugates during their biotransformation.
Keyword Aminotransferase
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ
Additional Notes Article first published online: 12 April 2011. 1996 Royal Pharmaceutical Society of Great Britain

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Pharmacy Publications
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Created: Mon, 20 Dec 2010, 14:03:20 EST