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Journal Abstract Search


140 related items for PubMed ID: 9276671

  • 1. Enzyme flexibility: a new concept in recognition of hydrophobic substrates.
    Kawaguchi S, Nobe Y, Yasuoka J, Wakamiya T, Kusumoto S, Kuramitsu S.
    J Biochem; 1997 Jul; 122(1):55-63. PubMed ID: 9276671
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  • 2. Thermodynamics and molecular simulation analysis of hydrophobic substrate recognition by aminotransferases.
    Kawaguchi Si, Kuramitsu S.
    J Biol Chem; 1998 Jul 17; 273(29):18353-64. PubMed ID: 9660802
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  • 3. Construction of aminotransferase chimeras and analysis of their substrate specificity.
    Miyazawa K, Kawaguchi S, Okamoto A, Kato R, Ogawa T, Kuramitsu S.
    J Biochem; 1994 Mar 17; 115(3):568-77. PubMed ID: 8056774
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  • 4. Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase.
    Hayashi H, Inoue K, Nagata T, Kuramitsu S, Kagamiyama H.
    Biochemistry; 1993 Nov 16; 32(45):12229-39. PubMed ID: 8218300
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  • 8. Molecular analysis of the role of two aromatic aminotransferases and a broad-specificity aspartate aminotransferase in the aromatic amino acid metabolism of Pyrococcus furiosus.
    Ward DE, de Vos WM, van der Oost J.
    Archaea; 2002 Sep 16; 1(2):133-41. PubMed ID: 15803651
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  • 10. Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme.
    Okada K, Hirotsu K, Hayashi H, Kagamiyama H.
    Biochemistry; 2001 Jun 26; 40(25):7453-63. PubMed ID: 11412098
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  • 11. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.
    Onuffer JJ, Ton BT, Klement I, Kirsch JF.
    Protein Sci; 1995 Sep 26; 4(9):1743-9. PubMed ID: 8528072
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  • 12. Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
    Onuffer JJ, Kirsch JF.
    Protein Sci; 1995 Sep 26; 4(9):1750-7. PubMed ID: 8528073
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  • 13. Dual substrate recognition of aminotransferases.
    Hirotsu K, Goto M, Okamoto A, Miyahara I.
    Chem Rec; 2005 Sep 26; 5(3):160-72. PubMed ID: 15889412
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  • 14. Significant improvement to the catalytic properties of aspartate aminotransferase: role of hydrophobic and charged residues in the substrate binding pocket.
    Köhler E, Seville M, Jäger J, Fotheringham I, Hunter M, Edwards M, Jansonius JN, Kirschner K.
    Biochemistry; 1994 Jan 11; 33(1):90-7. PubMed ID: 7904477
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  • 15. Aspartate aminotransferase of E. coli: effects of site-directed mutagenesis on substrate recognition.
    Kagamiyama H.
    J Nutr Sci Vitaminol (Tokyo); 1992 Jan 11; Spec No():216-9. PubMed ID: 1297744
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  • 16. Crystal structures of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network.
    Okamoto A, Nakai Y, Hayashi H, Hirotsu K, Kagamiyama H.
    J Mol Biol; 1998 Jul 17; 280(3):443-61. PubMed ID: 9665848
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  • 17. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8.
    Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S.
    J Biochem; 1996 Jan 17; 119(1):135-44. PubMed ID: 8907187
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  • 18. Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.
    Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H.
    J Biochem; 1991 Apr 17; 109(4):570-6. PubMed ID: 1869510
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  • 19. [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.
    Hayashi H, Kuramitsu S, Inoue Y, Morino Y, Kagamiyama H.
    Biochem Biophys Res Commun; 1989 Feb 28; 159(1):337-42. PubMed ID: 2564274
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  • 20. Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.
    Chen CD, Lin CH, Chuankhayan P, Huang YC, Hsieh YC, Huang TF, Guan HH, Liu MY, Chang WC, Chen CJ.
    J Bacteriol; 2012 Nov 28; 194(22):6206-16. PubMed ID: 22984263
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