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Journal Abstract Search

111 related items for PubMed ID: 1297744

  • 1. Aspartate aminotransferase of E. coli: effects of site-directed mutagenesis on substrate recognition.
    Kagamiyama H.
    J Nutr Sci Vitaminol (Tokyo); 1992; Spec No():216-9. PubMed ID: 1297744
    [Abstract] [Full Text] [Related]

  • 2. Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
    Vacca RA, Christen P, Malashkevich VN, Jansonius JN, Sandmeier E.
    Eur J Biochem; 1995 Jan 15; 227(1-2):481-7. PubMed ID: 7851426
    [Abstract] [Full Text] [Related]

  • 3. Replacement of an interdomain residue Val39 of Escherichia coli aspartate aminotransferase affects the catalytic competence without altering the substrate specificity of the enzyme.
    Hayashi H, Kuramitsu S, Kagamiyama H.
    J Biochem; 1991 May 15; 109(5):699-704. PubMed ID: 1917893
    [Abstract] [Full Text] [Related]

  • 4. Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.
    Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Kagamiyama H.
    Biochemistry; 1991 Aug 06; 30(31):7796-801. PubMed ID: 1868057
    [Abstract] [Full Text] [Related]

  • 5. 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 06; 109(4):570-6. PubMed ID: 1869510
    [Abstract] [Full Text] [Related]

  • 6. Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.
    Vacca RA, Giannattasio S, Graber R, Sandmeier E, Marra E, Christen P.
    J Biol Chem; 1997 Aug 29; 272(35):21932-7. PubMed ID: 9268327
    [Abstract] [Full Text] [Related]

  • 7. [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
    [Abstract] [Full Text] [Related]

  • 8. 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 28; 4(9):1750-7. PubMed ID: 8528073
    [Abstract] [Full Text] [Related]

  • 9. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
    Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H.
    Biochemistry; 1992 Jun 30; 31(25):5878-87. PubMed ID: 1610831
    [Abstract] [Full Text] [Related]

  • 10. The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.
    Yano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H.
    J Biol Chem; 1991 Apr 05; 266(10):6079-85. PubMed ID: 2007566
    [Abstract] [Full Text] [Related]

  • 11. Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.
    Hayashi H, Inoue Y, Kuramitsu S, Morino Y, Kagamiyama H.
    Biochem Biophys Res Commun; 1990 Mar 16; 167(2):407-12. PubMed ID: 2182010
    [Abstract] [Full Text] [Related]

  • 12. The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8.
    Nobe Y, Kawaguchi S, Ura H, Nakai T, Hirotsu K, Kato R, Kuramitsu S.
    J Biol Chem; 1998 Nov 06; 273(45):29554-64. PubMed ID: 9792664
    [Abstract] [Full Text] [Related]

  • 13. 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 06; 4(9):1743-9. PubMed ID: 8528072
    [Abstract] [Full Text] [Related]

  • 14. Substitution of a lysyl residue for arginine 386 of Escherichia coli aspartate aminotransferase.
    Inoue Y, Kuramitsu S, Inoue K, Kagamiyama H, Hiromi K, Tanase S, Morino Y.
    J Biol Chem; 1989 Jun 05; 264(16):9673-81. PubMed ID: 2498335
    [Abstract] [Full Text] [Related]

  • 15. Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity.
    Kuramitsu S, Hiromi K, Hayashi H, Morino Y, Kagamiyama H.
    Biochemistry; 1990 Jun 12; 29(23):5469-76. PubMed ID: 2201406
    [Abstract] [Full Text] [Related]

  • 16. 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 12; 122(1):55-63. PubMed ID: 9276671
    [Abstract] [Full Text] [Related]

  • 17. 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
    [Abstract] [Full Text] [Related]

  • 18. Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.
    Rothman SC, Voorhies M, Kirsch JF.
    Protein Sci; 2004 Mar 11; 13(3):763-72. PubMed ID: 14767072
    [Abstract] [Full Text] [Related]

  • 19. The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
    Almo SC, Smith DL, Danishefsky AT, Ringe D.
    Protein Eng; 1994 Mar 11; 7(3):405-12. PubMed ID: 7909946
    [Abstract] [Full Text] [Related]

  • 20. Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
    Mouratou B, Kasper P, Gehring H, Christen P.
    J Biol Chem; 1999 Jan 15; 274(3):1320-5. PubMed ID: 9880502
    [Abstract] [Full Text] [Related]

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