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Journal Abstract Search

123 related items for PubMed ID: 8188643

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  • 4. Mutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties.
    Ziak M, Jäger J, Malashkevich VN, Gehring H, Jaussi R, Jansonius JN, Christen P.
    Eur J Biochem; 1993 Feb 01; 211(3):475-84. PubMed ID: 8436109
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  • 5. 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
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  • 6. 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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  • 7. 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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  • 10. 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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  • 12. Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine.
    Nishimura K, Tanizawa K, Yoshimura T, Esaki N, Futaki S, Manning JM, Soda K.
    Biochemistry; 1991 Apr 23; 30(16):4072-7. PubMed ID: 1902115
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  • 13. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
    Jeffery CJ, Gloss LM, Petsko GA, Ringe D.
    Protein Eng; 2000 Feb 23; 13(2):105-12. PubMed ID: 10708649
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  • 18. Identification of lysine 346 as a functionally important residue for pyridoxal 5'-phosphate binding and catalysis in lysine 2, 3-aminomutase from Bacillus subtilis.
    Chen D, Frey PA.
    Biochemistry; 2001 Jan 16; 40(2):596-602. PubMed ID: 11148055
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  • 19. Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
    Gloss LM, Kirsch JF.
    Biochemistry; 1995 Sep 26; 34(38):12323-32. PubMed ID: 7547975
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  • 20. Site-specific methylation of a strategic lysyl residue in aspartate aminotransferase.
    Roberts WJ, Hubert E, Iriarte A, Martinez-Carrion M.
    J Biol Chem; 1988 May 25; 263(15):7196-202. PubMed ID: 3130380
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