PMID:353051
| Citation |
Maitra, US and Sprinson, DB (1978) 5-Dehydro-3-deoxy-D-arabino-heptulosonic acid 7-phosphate. An intermediate in the 3-dehydroquinate synthase reaction. J. Biol. Chem. 253:5426-30 |
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| Abstract |
3-Dehydroquinate synthase was purified to homogeneity from Escherichia coli. It was found to be a single polypeptide chain of Mr = approximately 57,000. Reaction mixtures of pure enzyme and the substrate, 3-deoxy-D-arabino-heptulosonic acid 7-phosphate, were incubated for short times and treated with NaB3H4. The resulting 3-deoxyheptonic acid 7-phosphate was degraded with sodium periodate, and formic acid representing C-5 of the substrate was isolated. The presence of 3H in the formate corresponding to 15% of the enzyme was interpreted as indicating a 5-dehydro derivative of the substrate as an intermediate of the reaction. Quinic acid, resulting from reduction of 3-dehydroquinate with NaB3H4, was also isolated and degraded with periodate. The formate from C-4 of the quinate was unlabeled, indicating that 3,4-bisdehydroquinate is not an intermediate. |
| Links | |
| Keywords |
Borohydrides/pharmacology; Escherichia coli/enzymology; Heptoses; Kinetics; Ligases/isolation & purification; Ligases/metabolism; Molecular Weight; Quinic Acid/analogs & derivatives; Sugar Acids |
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