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Journal Abstract Search

194 related items for PubMed ID: 27319381

  • 1.
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  • 2. Large scale dynamics of the Michaelis complex in Bacillus stearothermophilus lactate dehydrogenase revealed by a single-tryptophan mutant study.
    Nie B, Deng H, Desamero R, Callender R.
    Biochemistry; 2013 Mar 19; 52(11):1886-92. PubMed ID: 23428201
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  • 3. The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway.
    McClendon S, Zhadin N, Callender R.
    Biophys J; 2005 Sep 19; 89(3):2024-32. PubMed ID: 15980172
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  • 4. Lactate dehydrogenase undergoes a substantial structural change to bind its substrate.
    Qiu L, Gulotta M, Callender R.
    Biophys J; 2007 Sep 01; 93(5):1677-86. PubMed ID: 17483169
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  • 5. Evidence for temperature-dependent conformational changes in the L-lactate dehydrogenase from Bacillus stearothermophilus.
    Kotik M, Zuber H.
    Biochemistry; 1992 Sep 01; 31(34):7787-95. PubMed ID: 1510965
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  • 6. Slow structural changes shown by the 3-nitrotyrosine-237 residue in pig heart [Tyr(3NO2)237] lactate dehydrogenase.
    Parker DM, Jeckel D, Holbrook JJ.
    Biochem J; 1982 Mar 01; 201(3):465-71. PubMed ID: 7092806
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  • 7. A double mutant of highly purified Geobacillus stearothermophilus lactate dehydrogenase recognises l-mandelic acid as a substrate.
    Binay B, Sessions RB, Karagüler NG.
    Enzyme Microb Technol; 2013 May 10; 52(6-7):393-9. PubMed ID: 23608509
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  • 8. Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme.
    Cameron AD, Roper DI, Moreton KM, Muirhead H, Holbrook JJ, Wigley DB.
    J Mol Biol; 1994 May 13; 238(4):615-25. PubMed ID: 8176749
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  • 10. Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH.
    Karagüler NG, Sessions RB, Binay B, Ordu EB, Clarke AR.
    Biochem Soc Trans; 2007 Dec 13; 35(Pt 6):1610-5. PubMed ID: 18031276
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  • 11. Guided evolution of enzymes with new substrate specificities.
    el Hawrani AS, Sessions RB, Moreton KM, Holbrook JJ.
    J Mol Biol; 1996 Nov 22; 264(1):97-110. PubMed ID: 8950270
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  • 15. An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.
    Clarke AR, Wilks HM, Barstow DA, Atkinson T, Chia WN, Holbrook JJ.
    Biochemistry; 1988 Mar 08; 27(5):1617-22. PubMed ID: 3365414
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  • 16. Semi-Rational Design of Geobacillus stearothermophilus L-Lactate Dehydrogenase to Access Various Chiral α-Hydroxy Acids.
    Aslan AS, Birmingham WR, Karagüler NG, Turner NJ, Binay B.
    Appl Biochem Biotechnol; 2016 Jun 08; 179(3):474-84. PubMed ID: 26852025
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  • 17. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.
    Wilks HM, Hart KW, Feeney R, Dunn CR, Muirhead H, Chia WN, Barstow DA, Atkinson T, Clarke AR, Holbrook JJ.
    Science; 1988 Dec 16; 242(4885):1541-4. PubMed ID: 3201242
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  • 20. Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase.
    Deng H, Vu DV, Clinch K, Desamero R, Dyer RB, Callender R.
    J Phys Chem B; 2011 Jun 16; 115(23):7670-8. PubMed ID: 21568287
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