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3-Dehydroquinate synthase in germinating Phaseolus mungo seedlings
Journal of Biochemistry
|September 1, 1976
Summary
Dehydroquinate synthase was found in etiolated mung bean seedlings. This enzyme requires NAD+ and Co2+ to convert 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) into 3-dehydroquinate.
Area of Science:
- Biochemistry
- Plant Physiology
- Enzymology
Background:
- Dehydroquinate synthase is a key enzyme in the shikimate pathway.
- The shikimate pathway is essential for the biosynthesis of aromatic compounds in plants.
- Understanding plant enzyme function is crucial for agricultural and biotechnological applications.
Purpose of the Study:
- To detect dehydroquinate synthase activity in etiolated Phaseolus mungo seedlings.
- To characterize the cofactors required for enzyme activity.
- To identify the reaction product using radiolabeling techniques.
Main Methods:
- Preparation of cell-free extracts from etiolated Phaseolus mungo seedlings.
- Enzymatic assay using [1-14C]DAHP as substrate.
- Product identification via paper-radiochromatography.
- Testing the effect of NAD+ and Co2+ on enzyme activity.
Main Results:
- Dehydroquinate synthase activity was detected in the cell-free extracts.
- The enzyme catalyzed the conversion of [1-14C]DAHP to 3-dehydroquinate.
- Enzyme activity was dependent on the presence of NAD+ and Co2+.
- The reaction product was confirmed by paper-radiochromatography.
Conclusions:
- Dehydroquinate synthase is present and active in etiolated Phaseolus mungo seedlings.
- NAD+ and Co2+ are essential cofactors for the activity of this enzyme.
- This finding contributes to the understanding of aromatic compound biosynthesis in plants.