The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes.
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Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN
The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes.
Hum Exp Toxicol. 1995 May;14(5):422-7. doi: 10.1177/096032719501400506.
- PubMed ID
- 7612304 [ View in PubMed]
- Abstract
One biotransformation pathway which is responsible for the generation of mutagenic and cytotoxic metabolites is that of the C-S lysis (CSL) of L-cysteine conjugates. Thirteen cysteine S-conjugates, synthesised in our laboratories, were incubated with porcine heart aspartate aminotransferase (ASAT) and alanine aminotransferase (ALAT), and the C-S lyase activity for each enzyme-substrate combination was determined. ASAT and ALAT were shown to exhibit CSL activity. It was also demonstrated that this activity was inhibited in the presence of the pyridoxal phosphate (PLP)-dependent enzyme inhibitor amino(oxyacetic acid) (AOAA) confirming the pyridoxal phosphate dependent mechanism by which C-S lysis is known to take place. Since the activities of these enzymes are used as biomarkers for the assessment of organ damage, the potential interaction of L-cysteine conjugates with them may suppress their activity through direct inhibition.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Cysteine Aspartate aminotransferase, cytoplasmic Protein Humans UnknownSubstrateDetails Cysteine Aspartate aminotransferase, mitochondrial Protein Humans UnknownSubstrateDetails