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59 related items for PubMed ID: 20107768

  • 41. Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily.
    Frantom PA.
    Arch Biochem Biophys; 2012 Mar 15; 519(2):202-9. PubMed ID: 22033339
    [Abstract] [Full Text] [Related]

  • 42. Molecular architecture of the acetohydroxyacid synthase holoenzyme.
    Zhang Y, Li Y, Liu X, Sun J, Li X, Lin J, Yang X, Xi Z, Shen Y.
    Biochem J; 2020 Jul 17; 477(13):2439-2449. PubMed ID: 32538427
    [Abstract] [Full Text] [Related]

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  • 44. Evolution-guided adaptation of an adenylation domain substrate specificity to an unusual amino acid.
    Vobruba S, Kadlcik S, Gazak R, Janata J.
    PLoS One; 2017 Jul 17; 12(12):e0189684. PubMed ID: 29240815
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  • 46. Subunit-subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition.
    Kyselková M, Janata J, Ságová-Marecková M, Kopecký J.
    Arch Microbiol; 2010 Mar 17; 192(3):195-200. PubMed ID: 20107768
    [Abstract] [Full Text] [Related]

  • 47. Mutations in two distinct regions of acetolactate synthase regulatory subunit from Streptomyces cinnamonensis result in the lack of sensitivity to end-product inhibition.
    Kopecký J, Janata J, Pospísil S, Felsberg J, Spízek J.
    Biochem Biophys Res Commun; 1999 Dec 09; 266(1):162-6. PubMed ID: 10581183
    [Abstract] [Full Text] [Related]

  • 48. Deregulation of acetohydroxy-acid synthase: Loss of allosteric inhibition conferred by mutations in the catalytic subunit.
    Kopecký J, Kyselková M, Sigutová L, Pospísil S, Felsberg J, Spízek J, Janata J.
    Folia Microbiol (Praha); 2008 Dec 09; 53(6):467-71. PubMed ID: 19381469
    [Abstract] [Full Text] [Related]

  • 49. Acetohydroxyacid synthase: a proposed structure for regulatory subunits supported by evidence from mutagenesis.
    Mendel S, Elkayam T, Sella C, Vinogradov V, Vyazmensky M, Chipman DM, Barak Z.
    J Mol Biol; 2001 Mar 16; 307(1):465-77. PubMed ID: 11243831
    [Abstract] [Full Text] [Related]

  • 50. Allosteric regulation in Acetohydroxyacid Synthases (AHASs)--different structures and kinetic behavior in isozymes in the same organisms.
    Barak Z, Chipman DM.
    Arch Biochem Biophys; 2012 Mar 15; 519(2):167-74. PubMed ID: 22198286
    [Abstract] [Full Text] [Related]

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  • 52. Mutations in two distinct regions of acetolactate synthase regulatory subunit from Streptomyces cinnamonensis result in the lack of sensitivity to end-product inhibition.
    Kopecký J, Janata J, Pospísil S, Felsberg J, Spízek J.
    Biochem Biophys Res Commun; 1999 Dec 09; 266(1):162-6. PubMed ID: 10581183
    [Abstract] [Full Text] [Related]

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  • 55. Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli.
    Kaplun A, Vyazmensky M, Zherdev Y, Belenky I, Slutzker A, Mendel S, Barak Z, Chipman DM, Shaanan B.
    J Mol Biol; 2006 Mar 31; 357(3):951-63. PubMed ID: 16458324
    [Abstract] [Full Text] [Related]

  • 56. Subunit-subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition.
    Kyselková M, Janata J, Ságová-Marecková M, Kopecký J.
    Arch Microbiol; 2010 Mar 31; 192(3):195-200. PubMed ID: 20107768
    [Abstract] [Full Text] [Related]

  • 57.
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  • 59. Allosteric regulation in Acetohydroxyacid Synthases (AHASs)--different structures and kinetic behavior in isozymes in the same organisms.
    Barak Z, Chipman DM.
    Arch Biochem Biophys; 2012 Mar 15; 519(2):167-74. PubMed ID: 22198286
    [Abstract] [Full Text] [Related]

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