Open AccessProperties and Regulation of Aspartate Kinase from Barley Seedlings (Hordeum vulgare L.)
Author(s) -
Peter R. Shewry,
Benjamin J. Miflin
Publication year - 1977
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.59.1.69
Subject(s) - hordeum vulgare , biology , hordeum , botany , agronomy , poaceae
Aspartate kinase (EC 2.7.2.4) has been purified 8-fold and characterized from germinating barley (Hordeum vulgare) seedlings. The enzyme is inhibited 50% by 0.7 mm l-lysine and almost completely at 5 mm. l-Methionine does not affect the enzyme on its own, but at low concentrations (0.1-1 mm) increases the inhibition in the presence of lysine, indicating that the two amino acids act as cooperative feedback regulators.
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