BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

573 related articles for article (PubMed ID: 9790670)

  • 1. 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]  

  • 2. 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]  

  • 3. Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step.
    Islam MM; Goto M; Miyahara I; Ikushiro H; Hirotsu K; Hayashi H
    Biochemistry; 2005 Jun; 44(23):8218-29. PubMed ID: 15938611
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Transient-state kinetics of the reaction of aspartate aminotransferase with aspartate at low pH reveals dual routes in the enzyme-substrate association process.
    Hayashi H; Kagamiyama H
    Biochemistry; 1997 Nov; 36(44):13558-69. PubMed ID: 9354624
    [TBL] [Abstract][Full Text] [Related]  

  • 5. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst.
    Rege VD; Kredich NM; Tai CH; Karsten WE; Schnackerz KD; Cook PF
    Biochemistry; 1996 Oct; 35(41):13485-93. PubMed ID: 8873618
    [TBL] [Abstract][Full Text] [Related]  

  • 6. 15N nuclear magnetic resonance studies of acid-base properties of pyridoxal-5'-phosphate aldimines in aqueous solution.
    Sharif S; Huot MC; Tolstoy PM; Toney MD; Jonsson KH; Limbach HH
    J Phys Chem B; 2007 Apr; 111(15):3869-76. PubMed ID: 17388551
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis.
    Iwasaki M; Hayashi H; Kagamiyama H
    J Biochem; 1994 Jan; 115(1):156-61. PubMed ID: 8188625
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 40(2):353-60. PubMed ID: 11148029
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle.
    Ikushiro H; Hayashi H; Kawata Y; Kagamiyama H
    Biochemistry; 1998 Mar; 37(9):3043-52. PubMed ID: 9485457
    [TBL] [Abstract][Full Text] [Related]  

  • 10. NMR studies of protonation and hydrogen bond states of internal aldimines of pyridoxal 5'-phosphate acid-base in alanine racemase, aspartate aminotransferase, and poly-L-lysine.
    Chan-Huot M; Dos A; Zander R; Sharif S; Tolstoy PM; Compton S; Fogle E; Toney MD; Shenderovich I; Denisov GS; Limbach HH
    J Am Chem Soc; 2013 Dec; 135(48):18160-75. PubMed ID: 24147985
    [TBL] [Abstract][Full Text] [Related]  

  • 11. A QM/MM simulation study of transamination reaction at the active site of aspartate aminotransferase: Free energy landscape and proton transfer pathways.
    Dutta Banik S; Bankura A; Chandra A
    J Comput Chem; 2020 Dec; 41(32):2684-2694. PubMed ID: 32932551
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes.
    Chattopadhyay A; Meier M; Ivaninskii S; Burkhard P; Speroni F; Campanini B; Bettati S; Mozzarelli A; Rabeh WM; Li L; Cook PF
    Biochemistry; 2007 Jul; 46(28):8315-30. PubMed ID: 17583914
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
    Sivaraman J; Li Y; Larocque R; Schrag JD; Cygler M; Matte A
    J Mol Biol; 2001 Aug; 311(4):761-76. PubMed ID: 11518529
    [TBL] [Abstract][Full Text] [Related]  

  • 14. NMR studies of the stability, protonation States, and tautomerism of (13)C- AND (15)N-labeled aldimines of the coenzyme pyridoxal 5'-phosphate in water.
    Chan-Huot M; Sharif S; Tolstoy PM; Toney MD; Limbach HH
    Biochemistry; 2010 Dec; 49(51):10818-30. PubMed ID: 21067170
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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]  

  • 16. 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]  

  • 17. Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine.
    Stamper GF; Morollo AA; Ringe D
    Biochemistry; 1998 Jul; 37(29):10438-45. PubMed ID: 9671513
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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]  

  • 19. Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base.
    Evande R; Ojha S; Banerjee R
    Arch Biochem Biophys; 2004 Jul; 427(2):188-96. PubMed ID: 15196993
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms.
    Jäger J; Moser M; Sauder U; Jansonius JN
    J Mol Biol; 1994 Jun; 239(2):285-305. PubMed ID: 8196059
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 29.