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The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4′-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity
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Cristallographic study of tyrosine phenol-lyase from Erwinia herbicola
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+ bound at this site inactivates the enzyme. The structure of the enzyme as a whole and its active site are thoroughly compared with those of other enzymes of the aspartate aminotransferase family.
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Cristallographic study of steps along the reaction pathway of D-amino acid aminotransferase
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0030800147
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2 complex with ligands bound to the active sites of the α-and β-subunits reveal ligand-induced conformational changes
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2 tetramer in which a ligand is bound to either only the α subunit active site, only the β subunit active site or to both sites are compared. This gives some clues to the triggering of the allosteric effects.
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0032502775
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2 complex reveals the correct orientation of active site αGlu49
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2 tetramer containing inactive α subunits (due to the mutation αD60N) complexed with the real indole-3-glycerol phosphate substrate reveals αGlu49 in its expected productive conformation.
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Mutations in the contact region between the α and β subunits of tryptophan synthase alter subunit interaction and intersubunit communication
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48. Rowlett R, Yang L-H, Ahmed SA, McPhie P, Jhee K-H, Wilson Miles E: Mutations in the contact region between the α and β subunits of tryptophan synthase alter subunit interaction and intersubunit communication. Biochemistry 1998, 37:2961-2968.
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