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Purification of two forms of the associated 3-dehydroquinate hydro-lyase and shikimate:NADP+oxidoreductase inPhaseolus mungoseedlings

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Enzymology
0005-2744
Publisher
Elsevier
Publication Date
Volume
522
Issue
1
Identifiers
DOI: 10.1016/0005-2744(78)90317-0
Disciplines
  • Biology

Abstract

Abstract Two associated enzymes, 3-dehydroquinate hydro-lyase (EC 4.2.1.10) and shikimate:NADP + oxidoreductase (EC 1.1.1.25), have been purified from Phaseolus mungo seedlings. These enzymes were purified 6900- and 9700-fold, respectively, but they were not separable. Moreover, two activity bands of the shikimate:NADP + oxidoreductase were detected after polyacrylamide gel electrophoresis and the two peaks also have 3-dehydroquinate hydro-lyase activity. The two forms of the associated enzymes showed only small differences in molecular weight, K m value, pH optimum and the responses to some inhibitors.

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