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Journal Abstract Search

273 related items for PubMed ID: 18314961

  • 1. Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects.
    Chakraborty S, Nemeria N, Yep A, McLeish MJ, Kenyon GL, Jordan F.
    Biochemistry; 2008 Mar 25; 47(12):3800-9. PubMed ID: 18314961
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  • 2. Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase.
    Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F.
    Biochemistry; 2009 Feb 10; 48(5):981-94. PubMed ID: 19140682
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  • 3. Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states.
    Nemeria N, Korotchkina L, McLeish MJ, Kenyon GL, Patel MS, Jordan F.
    Biochemistry; 2007 Sep 18; 46(37):10739-44. PubMed ID: 17715948
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  • 4. Structural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least motion mechanism with an unprecedented short-lived predecarboxylation intermediate.
    Bruning M, Berheide M, Meyer D, Golbik R, Bartunik H, Liese A, Tittmann K.
    Biochemistry; 2009 Apr 21; 48(15):3258-68. PubMed ID: 19182954
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  • 8. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens.
    Mosbacher TG, Mueller M, Schulz GE.
    FEBS J; 2005 Dec 21; 272(23):6067-76. PubMed ID: 16302970
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  • 9. Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I.
    González B, Vicuña R.
    J Bacteriol; 1989 May 21; 171(5):2401-5. PubMed ID: 2496105
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  • 11. Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme.
    Nemeria N, Baykal A, Joseph E, Zhang S, Yan Y, Furey W, Jordan F.
    Biochemistry; 2004 Jun 01; 43(21):6565-75. PubMed ID: 15157089
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  • 12. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase.
    Polovnikova ES, McLeish MJ, Sergienko EA, Burgner JT, Anderson NL, Bera AK, Jordan F, Kenyon GL, Hasson MS.
    Biochemistry; 2003 Feb 25; 42(7):1820-30. PubMed ID: 12590569
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  • 14. Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase.
    Sergienko EA, Wang J, Polovnikova L, Hasson MS, McLeish MJ, Kenyon GL, Jordan F.
    Biochemistry; 2000 Nov 14; 39(45):13862-9. PubMed ID: 11076527
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  • 15. Mechanistic kinetic model for symmetric carboligations using benzaldehyde lyase.
    Zavrel M, Schmidt T, Michalik C, Ansorge-Schumacher M, Marquardt W, Büchs J, Spiess AC.
    Biotechnol Bioeng; 2008 Sep 01; 101(1):27-38. PubMed ID: 18404768
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  • 17. Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.
    Brandt GS, Kneen MM, Petsko GA, Ringe D, McLeish MJ.
    J Am Chem Soc; 2010 Jan 20; 132(2):438-9. PubMed ID: 20030408
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  • 20. Accelerating unimolecular decarboxylation by preassociated acid catalysis in thiamin-derived intermediates: implicating Brønsted acids as carbanion traps in enzymes.
    Kluger R, Ikeda G, Hu Q, Cao P, Drewry J.
    J Am Chem Soc; 2006 Dec 13; 128(49):15856-64. PubMed ID: 17147398
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