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254 related items for PubMed ID: 8198554

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  • 6. Active site mutants of pyruvate decarboxylase from Zymomonas mobilis--a site-directed mutagenesis study of L112, I472, I476, E473, and N482.
    Pohl M, Siegert P, Mesch K, Bruhn H, Grötzinger J.
    Eur J Biochem; 1998 Nov 01; 257(3):538-46. PubMed ID: 9839941
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  • 7. Mutagenesis at asp27 of pyruvate decarboxylase from Zymomonas mobilis. Effect on its ability to form acetoin and acetolactate.
    Wu YG, Chang AK, Nixon PF, Li W, Duggleby RG.
    Eur J Biochem; 2000 Nov 01; 267(21):6493-500. PubMed ID: 11029594
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  • 8. Aspartate-27 and glutamate-473 are involved in catalysis by Zymomonas mobilis pyruvate decarboxylase.
    Chang AK, Nixon PF, Duggleby RG.
    Biochem J; 1999 Apr 15; 339 ( Pt 2)(Pt 2):255-60. PubMed ID: 10191255
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  • 11. Theoretical Studies of the Electronic Absorption Spectra of Thiamin Diphosphate in Pyruvate Decarboxylase.
    Paulikat M, Wechsler C, Tittmann K, Mata RA.
    Biochemistry; 2017 Apr 04; 56(13):1854-1864. PubMed ID: 28296385
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  • 12. Cofactor activation and substrate binding in pyruvate decarboxylase. Insights into the reaction mechanism from molecular dynamics simulations.
    Lie MA, Celik L, Jørgensen KA, Schiøtt B.
    Biochemistry; 2005 Nov 15; 44(45):14792-806. PubMed ID: 16274227
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  • 13. Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on wild-type indolepyruvate decarboxylase and variants using indolepyruvate, benzoylformate, and pyruvate as substrates.
    Schütz A, Golbik R, König S, Hübner G, Tittmann K.
    Biochemistry; 2005 Apr 26; 44(16):6164-79. PubMed ID: 15835904
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  • 17. Double duty for a conserved glutamate in pyruvate decarboxylase: evidence of the participation in stereoelectronically controlled decarboxylation and in protonation of the nascent carbanion/enamine intermediate .
    Meyer D, Neumann P, Parthier C, Friedemann R, Nemeria N, Jordan F, Tittmann K.
    Biochemistry; 2010 Sep 21; 49(37):8197-212. PubMed ID: 20715795
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  • 19. Site-directed mutagenesis of the ionizable groups in the active site of Zymomonas mobilis pyruvate decarboxylase: effect on activity and pH dependence.
    Huang CY, Chang AK, Nixon PF, Duggleby RG.
    Eur J Biochem; 2001 Jun 21; 268(12):3558-65. PubMed ID: 11422387
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  • 20. Steady-state kinetics and molecular evolution of Escherichia coli MenD [(1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase], an anomalous thiamin diphosphate-dependent decarboxylase-carboligase.
    Bhasin M, Billinsky JL, Palmer DR.
    Biochemistry; 2003 Nov 25; 42(46):13496-504. PubMed ID: 14621995
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