Succinylacetone Pyrrole, a Powerful Inhibitor of Vitamin B sub(12) Biosynthesis: Effect on delta -Aminolevulinic Acid Dehydratase

Succinylacetone, a competitive inhibitor (K sub(I) = 400 mu M) of delta -aminolevulinic acid dehydratase of Clostridium tetanomorphum), is converted non-enzymatically upon incubation with delta -aminolevulinic acid to succinylacetone pyrrole, a much stronger competitive inhibitor (K sub(I) = 5 mu M)...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 102; no. 3; pp. 854 - 859
Main Authors Brumm, P J, Friedmann, H C
Format Journal Article
LanguageEnglish
Published 01.01.1981
Subjects
biosynthesis
Clostridium tetanomorphum
porphobilinogen synthase
succinylacetone pyrrole
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Summary:Succinylacetone, a competitive inhibitor (K sub(I) = 400 mu M) of delta -aminolevulinic acid dehydratase of Clostridium tetanomorphum), is converted non-enzymatically upon incubation with delta -aminolevulinic acid to succinylacetone pyrrole, a much stronger competitive inhibitor (K sub(I) = 5 mu M) of the enzyme. A similar effect is seem in vivo: when present in the growth medium at concentrations of about 1 mu M, the pyrrole decrease the level of corrinoids produced by this organism by half, while succinylacetone at 200 mu M causes only 19 per cent inhibition of corrinoid formation. Levulinic acid is a much weaker inhibitor in vitro and in vivo. The inhibition by succinylacetone pyrrole is considered to be due to its structural resemblance to delta -aminolevulinic acid rather than to porphobilinogen, the reaction product of delta -aminolevulinic acid dehydratase: succinylacetone, succinylacetone pyrrole, and levulinic acid all contain a succinyl group.
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ISSN:0006-291X