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Purification and characterization of 5-aminolaevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain.

5-Aminolaevulinic acid dehydratase (ALAD) from a recombinant strain of Escherichia coli was purified to homogeneity. The enzyme is a homo-octamer of subunit M(r) 36554 +/- 17. Enzyme activity was dependent on the presence of Zn2+ ions and an exogenous thiol. Two molar equivalents of Zn2+ are bound/m...

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Bibliografiske detaljer
Main Authors: Spencer, P, Jordan, P M
Format: Artigo
Sprog:Inglês
Udgivet: 1993
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132412/
https://ncbi.nlm.nih.gov/pubmed/8439296
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