Lycorine: A powerful inhibitor of L-galactono-γ-lactone dehydrogenase activity
In vivo conversion of L-galactono-γ-lactone to ascorbate is carried out in all of the plants that we have analysed. The enzyme catalysing this reaction, i.e. L-galactono-γ-lactone dehydrogenase, which appears to be localised in the mitochondrial membrane, is strongly inhibited by lycorine: 5 μM lyco...
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Published in: | Journal of plant physiology Vol. 150; no. 3; pp. 362 - 364 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Jena
Elsevier GmbH
1997
Elsevier |
Subjects: | |
Online Access: | Get full text |
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Summary: | In vivo conversion of L-galactono-γ-lactone to ascorbate is carried out in all of the plants that we have analysed. The enzyme catalysing this reaction, i.e. L-galactono-γ-lactone dehydrogenase, which appears to be localised in the mitochondrial membrane, is strongly inhibited by lycorine: 5 μM lycorine almost completely inhibits the activity of the enzyme. The alkaloid does not affect the activity of the ascorbate free radical reductase, dehydroascorbate reductase or ascorbate peroxidase. The results presented here confirm that lycorine is a specific inhibitor of ascorbate biosynthesis in plants, and, consequently, that it can be a useful tool to bener understand the ascorbate metabolism in ascorbate synthesising organisms. |
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Bibliography: | 1998G50136 H50 |
ISSN: | 0176-1617 1618-1328 |
DOI: | 10.1016/S0176-1617(97)80134-4 |