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pubmed-article:16659791pubmed:abstractTextAspartate 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.lld:pubmed
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pubmed-article:16659791pubmed:authorpubmed-author:MiflinB JBJlld:pubmed
pubmed-article:16659791pubmed:authorpubmed-author:ShewryP RPRlld:pubmed
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pubmed-article:16659791pubmed:dateRevised2010-9-14lld:pubmed
pubmed-article:16659791pubmed:year1977lld:pubmed
pubmed-article:16659791pubmed:articleTitleProperties and Regulation of Aspartate Kinase from Barley Seedlings (Hordeum vulgare L.).lld:pubmed
pubmed-article:16659791pubmed:affiliationRothamsted Experimental Station, Harpenden, Herts. AL5 2JQ, United Kingdom.lld:pubmed
pubmed-article:16659791pubmed:publicationTypeJournal Articlelld:pubmed
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