# Metal‐Induced Alterations of δ‐Aminolevulinic Acid Dehydratase

@article{Bernard1987MetalInducedAO,
title={Metal‐Induced Alterations of $\delta$‐Aminolevulinic Acid Dehydratase},
author={A. Bernard and Robert Lauwerys},
journal={Annals of the New York Academy of Sciences},
year={1987},
volume={514}
}
• Published 1 December 1987
• Chemistry, Medicine
• Annals of the New York Academy of Sciences
ALAD is a cytoplasmic enzyme that catalyzes the second step of the heme biosynthesis pathway, that is, the condensation of two molecules of delta-aminolevulinic acid into porphobilinogen. ALAD is a zinc-dependent enzyme; thiol groups are essential for its activity; and in vitro experiments show that ALAD can be activated or inhibited by several metal ions including A;3+, Pb2+, Cd2+, Hg2+, Ag2+, and Cu2+. To explain these effects, it has been postulated that metals bind to thiol groups of…
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The effects of twelve metals at various concentrations ranging from 10(-41 to 10(-7) M) M have been studied on delta-aminolaevulinic acid dehydratase 9000 fold (ALA-D), isolated and purified from human red cells, and agree with the following hypothesis: according to their structure, metals would bind the enzyme in one or several allosteric sites, and induce an allosterics transposition to the active or inactive form of enzyme.
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