L-Malate: NADP oxidoreductase (decarboxylating) from germinating flax rust uredospores

l-Malate: NADP oxidoreductase (decarboxylating) (here called “malic” enzyme) from germinating flax rust uredospores was purified more than twenty-fold and partially characterized. This enzyme preparation was found to catalyze both the oxidative decarboxylation of l-malic acid to pyruvic acid at pH 7...

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Published inPhytochemistry (Oxford) Vol. 2; no. 1; pp. 75 - 83
Main Authors Johnson, M.A., Frear, D.S.
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.01.1963
Subjects
biosynthesis
enzyme activity
enzyme inhibitors
Linum usitatissimum
malate oxidase
Melampsora lini
NADP (coenzyme)
purification
spore germination
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Summary:l-Malate: NADP oxidoreductase (decarboxylating) (here called “malic” enzyme) from germinating flax rust uredospores was purified more than twenty-fold and partially characterized. This enzyme preparation was found to catalyze both the oxidative decarboxylation of l-malic acid to pyruvic acid at pH 7·6 and the decarboxylation of oxalacetic acid at pH 5. The oxidative decarboxylation of l-malate was found to specifically need NADP and required Mn 2+ for maximum activity. Optimal pH for enzyme activity was 7·6. A Michaelis constant for l-malate of 1·5 × 10 −4 M was found for this partially purified enzyme preparation. The stability and heat lability of the enzyme are reported in addition to the effect of a number of inhibitors.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(00)88019-X