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...
Saved in:
Published in | Phytochemistry (Oxford) Vol. 2; no. 1; pp. 75 - 83 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
01.01.1963
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 |