δ-Aminolevulinic acid dehydratase of Mycobacterium phlei

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Abstract

δ-Aminolevulinic acid dehydratase (5-aminolevulinate hydro-lyase (adding 5-aminolevulinate and cyclizing), EC 4.2.1.24) was purified 160-fold from crude extracts of Mycobacterium phlei. The pH optimum was 9.2; the Km value for δ-aminolevulinic acid was 7.7 · 10−5M. Mg2+ was necessary for the maximum activity of the enzyme and EDTA inhibited the activity markedly. δ-Hydroxylevulinic acid, δ-hydroxy-γ-oxo-l-norvaline and levulinic acid inhibited the enzyme activity competitively.

Inhibitory effect of α-ketoglutarate:glyoxylate carboligase activity on δ-aminolevulinic acid dehydratase activity was studied using the cell free extracts of M. phlei.

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