Substrate activation behaviour of pyruvate decarboxylase from Pisum sativum cv. Miko.
The substrate activation behaviour of pyruvate decarboxylase from germinating seeds of Pisum sativum is characterised kinetically via stopped-flow measurements and discussed with respect to other species. The involvement of SH-groups in this process is demonstrated by reference experiments with chemically modified enzyme.
Dietrich
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Martin-Luther-Universität Halle-Wittenberg, Fachbereich Biochemie/Biotechnologie, Institut für Biochemie, Halle/Saale, Germany.
König
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D004789:Enzyme Activation; D007887:Fabaceae / Q000201:enzymology*; D010946:Plants, Medicinal; D011767:Pyruvate Decarboxylase / Q000378:metabolism*; D011773:Pyruvates / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D011773:Pyruvates; D011767:Pyruvate Decarboxylase