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Issue 3, 1996
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Mechanism-based inhibition of 5-aminolaevulinic acid dehydratase from Bacillus subtilis by the 3-thia analogue of the substrate

Abstract

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

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Article type: Paper
DOI: 10.1039/CC9960000303
Citation: Chem. Commun., 1996,0, 303-304
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    Mechanism-based inhibition of 5-aminolaevulinic acid dehydratase from Bacillus subtilis by the 3-thia analogue of the substrate

    D. Appleton and F. J. Leeper, Chem. Commun., 1996, 0, 303
    DOI: 10.1039/CC9960000303

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