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313 related items for PubMed ID: 10708649

  • 1. 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; 13(2):105-12. PubMed ID: 10708649
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  • 2. 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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  • 3. Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
    Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H.
    Biochemistry; 2001 Jan 16; 40(2):353-60. PubMed ID: 11148029
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  • 4. 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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  • 5. 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 15; 7(3):405-12. PubMed ID: 7909946
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  • 11. Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.
    Eliot AC, Kirsch JF.
    Biochemistry; 2002 Mar 19; 41(11):3836-42. PubMed ID: 11888303
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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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  • 13. 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
    Smith DL, Almo SC, Toney MD, Ringe D.
    Biochemistry; 1989 Oct 03; 28(20):8161-7. PubMed ID: 2513875
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  • 14. Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms.
    Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM.
    Biochemistry; 2002 Oct 01; 41(39):11592-601. PubMed ID: 12269802
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  • 15. 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 01; 109(4):570-6. PubMed ID: 1869510
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  • 18. Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate.
    Scarsdale JN, Radaev S, Kazanina G, Schirch V, Wright HT.
    J Mol Biol; 2000 Feb 11; 296(1):155-68. PubMed ID: 10656824
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