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Abstract 79 The interaction of various substrate analogues with 5-aminolaevulinic acid dehydratase (porphobilinogen synthase) from Bacillus subtilis has been studied kinetically and by electrospray mass spectrometry; 5-chlorolaevulinic acid has been shown to be a non-specific alkylating agent but 5-amino-3-thialaevulinic acid is a potent mechanism-based inactivator.
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