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The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymesDepartment of Pharmaceutical Sciences, University of Nottingham, Nottingham, NG7 2RD
Department of Chemistry, De Montfort University, Leicester, LE1 9BH, UK
Department of Chemistry, De Montfort University, Leicester, LE1 9BH, UK
Department of Chemistry, De Montfort University, Leicester, LE1 9BH, UK
Department of Pharmaceutical Sciences, University of Nottingham, Nottingham, NG7 2RD 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 labora tories, were incubated with porcine heart aspartate aminotransferase (ASAT) and alanine aminotransferase (ALAT), and the C-S lyase activity for each enzyme-sub strate 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 pyri doxal 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 dam age, the potential interaction of L-cysteine conjugates with them may suppress their activity through direct inhibition.
Key Words: cysteine conjugate β-lyase • aspartate amino transferase • alanine amino transferase • porcine heart
Human & Experimental Toxicology, Vol. 14, No. 5,
422-427 (1995) This article has been cited by other articles:
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