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Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine Inra
Paris, S.; Viemon, C.; Curien, G.; Dumas, R..
The regulatory domain of the bifunctional threonine-sensitive aspartate kinase homoserine dehydrogenase contains two homologous subdomains defined by a common loop-αhelix-loop-β strand-loop-β strand motif. This motif is homologous with that found in the two subdomains of the biosynthetic threonine-deaminase regulatory domain. Comparisons of the primary and secondary structures of the two enzymes allowed us to predict the location and identity of the amino acid residues potentially involved in two threonine-binding sites ofArabidopsis thaliana aspartate kinase-homoserine dehydrogenase. These amino acids were then mutated and activity measurements were carried out to test this hypothesis. Steady-state kinetic experiments on the wild-type and mutant enzymes...
Tipo: Journal Article Palavras-chave: ASPARTOKINASE; GENE THRA; DESAMINASE; STRUCTURE ENZYMATIQUE; INHIBITION ENZYMATIQUE; SEQUENCE NUCLEOTIDIQUE; THREONINE.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400031090101858&uri=/notices/prodinra1/2010/11/
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