BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

802 related articles for article (PubMed ID: 1610831)

  • 1. 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; 31(25):5878-87. PubMed ID: 1610831
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog.
    Yano T; Hinoue Y; Chen VJ; Metzler DE; Miyahara I; Hirotsu K; Kagamiyama H
    J Mol Biol; 1993 Dec; 234(4):1218-29. PubMed ID: 8263922
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change.
    Onuffer JJ; Kirsch JF
    Protein Eng; 1994 Mar; 7(3):413-24. PubMed ID: 8177890
    [TBL] [Abstract][Full Text] [Related]  

  • 4. 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; 266(10):6079-85. PubMed ID: 2007566
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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; 211(3):475-84. PubMed ID: 8436109
    [TBL] [Abstract][Full Text] [Related]  

  • 6. A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase.
    Yano T; Mizuno T; Kagamiyama H
    Biochemistry; 1993 Feb; 32(7):1810-5. PubMed ID: 8439541
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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; 30(1):305-12. PubMed ID: 1988027
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 34(2):405-14. PubMed ID: 7819232
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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; 187(2):329-33. PubMed ID: 2105217
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor.
    Gong J; Hunter GA; Ferreira GC
    Biochemistry; 1998 Mar; 37(10):3509-17. PubMed ID: 9521672
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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; 109(4):570-6. PubMed ID: 1869510
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Crystal structures of aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate: internal aldimine and stable L-aspartate external aldimine.
    Griswold WR; Fisher AJ; Toney MD
    Biochemistry; 2011 Jul; 50(26):5918-24. PubMed ID: 21627105
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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; 37(43):15076-85. PubMed ID: 9790670
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase.
    Toney MD; Kirsch JF
    Biochemistry; 1991 Jul; 30(30):7461-6. PubMed ID: 1677270
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.
    Hayashi H; Mizuguchi H; Miyahara I; Nakajima Y; Hirotsu K; Kagamiyama H
    J Biol Chem; 2003 Mar; 278(11):9481-8. PubMed ID: 12488449
    [TBL] [Abstract][Full Text] [Related]  

  • 16. 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; 33(10):2757-60. PubMed ID: 8130187
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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; 227(1-2):481-7. PubMed ID: 7851426
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine.
    Gloss LM; Kirsch JF
    Biochemistry; 1995 Mar; 34(12):3990-8. PubMed ID: 7696264
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Replacement of active-site lysine-239 of thermostable aspartate aminotransferase by S-(2-aminoethyl)cysteine: properties of the mutant enzyme.
    Matsushima Y; Kim DW; Yoshimura T; Kuramitsu S; Kagamiyama H; Esaki N; Soda K
    J Biochem; 1994 Jan; 115(1):108-12. PubMed ID: 8188615
    [TBL] [Abstract][Full Text] [Related]  

  • 20. 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; 146(2):416-21. PubMed ID: 3113421
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 41.