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Journal Abstract Search

194 related items for PubMed ID: 2105217

  • 1. Aspartate aminotransferase with the pyridoxal-5'-phosphate-binding lysine residue replaced by histidine retains partial catalytic competence.
    Ziak M, Jaussi R, Gehring H, Christen P.
    Eur J Biochem; 1990 Jan 26; 187(2):329-33. PubMed ID: 2105217
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  • 3. Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
    Malashkevich VN, Jäger J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN.
    Biochemistry; 1995 Jan 17; 34(2):405-14. PubMed ID: 7819232
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  • 5. Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase.
    Kuramitsu S, Inoue Y, Tanase S, Morino Y, Kagamiyama H.
    Biochem Biophys Res Commun; 1987 Jul 31; 146(2):416-21. PubMed ID: 3113421
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  • 6. 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
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  • 7. 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
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  • 9. The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase.
    Grimm B, Smith MA, von Wettstein D.
    Eur J Biochem; 1992 Jun 01; 206(2):579-85. PubMed ID: 1597195
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  • 10. The stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate is abolished in (Lys258----Ala) aspartate aminotransferase.
    Kochhar S, Finlayson WL, Kirsch JF, Christen P.
    J Biol Chem; 1987 Aug 25; 262(24):11446-8. PubMed ID: 3114245
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  • 11. Spectroscopic characterization of true enzyme-substrate intermediates of aspartate aminotransferase trapped at subzero temperatures.
    Sterk M, Gehring H.
    Eur J Biochem; 1991 Nov 01; 201(3):703-7. PubMed ID: 1935964
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  • 12. The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.
    Goldberg JM, Swanson RV, Goodman HS, Kirsch JF.
    Biochemistry; 1991 Jan 08; 30(1):305-12. PubMed ID: 1988027
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  • 15. Shift in pH-rate profile and enhanced discrimination between dicarboxylic and aromatic substrates in mitochondrial aspartate aminotransferase Y70H.
    Pan P, Jaussi R, Gehring H, Giannattasio S, Christen P.
    Biochemistry; 1994 Mar 15; 33(10):2757-60. PubMed ID: 8130187
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  • 16. The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis.
    Hayashi H, Mizuguchi H, Kagamiyama H.
    Biochemistry; 1998 Oct 27; 37(43):15076-85. PubMed ID: 9790670
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  • 20. 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 27; 109(4):570-6. PubMed ID: 1869510
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