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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom