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Wounding Induces One of Two Isoenzymes of 3-Deoxy-d-arabino-Heptulosonate 7-Phosphate Synthase in Solanum tuberosum L.
Author(s) -
Gloria K. Muday,
Klaus M. Herrmann
Publication year - 1992
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.98.2.496
Subject(s) - isozyme , shikimate pathway , solanum tuberosum , biochemistry , atp synthase , enzyme , phosphofructokinase 2 , biology , aromatic amino acids , biosynthesis , polyclonal antibodies , divalent , chemistry , botany , antibody , genetics , organic chemistry
Potato (Solanum tuberosum L.) tubers contain two isoenzymes of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (EC 4.1.2.15), the enzyme that catalyzes the first step of aromatic amino acid biosynthesis. One of the isoenzymes is specifically activated by Mn(2+), and the other requires Co(2+), Mg(2+), or another divalent cation for activity. Monospecific polyclonal antibodies against the Mn(2+)-activated isoenzyme do not cross-react with the other isoenzyme. Wounding of potato tubers induces the Mn(2+)-activated form but not the other. We conclude that two different genes encode two different isoenzymes that catalyze the first step in the shikimate pathway.

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