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374 related items for PubMed ID: 16458324

  • 1. 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]

  • 2. 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]

  • 3. Interactions between large and small subunits of different acetohydroxyacid synthase isozymes of Escherichia coli.
    Vyazmensky M, Zherdev Y, Slutzker A, Belenky I, Kryukov O, Barak Z, Chipman DM.
    Biochemistry; 2009 Sep 15; 48(36):8731-7. PubMed ID: 19653643
    [Abstract] [Full Text] [Related]

  • 4. Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.
    Pang SS, Duggleby RG, Guddat LW.
    J Mol Biol; 2002 Mar 22; 317(2):249-62. PubMed ID: 11902841
    [Abstract] [Full Text] [Related]

  • 5. The minimum activation peptide from ilvH can activate the catalytic subunit of AHAS from different species.
    Zhao Y, Niu C, Wen X, Xi Z.
    Chembiochem; 2013 Apr 15; 14(6):746-52. PubMed ID: 23512804
    [Abstract] [Full Text] [Related]

  • 6. Homology modeling of the structure of bacterial acetohydroxy acid synthase and examination of the active site by site-directed mutagenesis.
    Ibdah M, Bar-Ilan A, Livnah O, Schloss JV, Barak Z, Chipman DM.
    Biochemistry; 1996 Dec 17; 35(50):16282-91. PubMed ID: 8973202
    [Abstract] [Full Text] [Related]

  • 7. Role of the C-terminal domain of the regulatory subunit of AHAS isozyme III: use of random mutagenesis with in vivo reconstitution (REM-ivrs).
    Slutzker A, Vyazmensky M, Chipman DM, Barak Z.
    Biochim Biophys Acta; 2011 Mar 17; 1814(3):449-55. PubMed ID: 21224018
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.
    Belenky I, Steinmetz A, Vyazmensky M, Barak Z, Tittmann K, Chipman DM.
    FEBS J; 2012 Jun 15; 279(11):1967-79. PubMed ID: 22443469
    [Abstract] [Full Text] [Related]

  • 10. Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme.
    Mitra A, Sarma SP.
    Biochemistry; 2008 Feb 12; 47(6):1518-31. PubMed ID: 18193896
    [Abstract] [Full Text] [Related]

  • 11. The coil-to-helix transition in IlvN regulates the allosteric control of Escherichia coli acetohydroxyacid synthase I.
    Karanth NM, Sarma SP.
    Biochemistry; 2013 Jan 08; 52(1):70-83. PubMed ID: 23205845
    [Abstract] [Full Text] [Related]

  • 12. Mutations in the regulatory subunit of yeast acetohydroxyacid synthase affect its activation by MgATP.
    Lee YT, Duggleby RG.
    Biochem J; 2006 Apr 15; 395(2):331-6. PubMed ID: 16390333
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  • 14. 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 15; 192(3):195-200. PubMed ID: 20107768
    [Abstract] [Full Text] [Related]

  • 15. Arginine 26 and aspartic acid 69 of the regulatory subunit are key residues of subunits interaction of acetohydroxyacid synthase isozyme III from E. coli.
    Zhao Y, Wen X, Niu C, Xi Z.
    Chembiochem; 2012 Nov 05; 13(16):2445-54. PubMed ID: 23047433
    [Abstract] [Full Text] [Related]

  • 16. The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli.
    Mendel S, Vinogradov M, Vyazmensky M, Chipman DM, Barak Z.
    J Mol Biol; 2003 Jan 10; 325(2):275-84. PubMed ID: 12488095
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  • 20. Structural and functional evaluation of three well-conserved serine residues in tobacco acetohydroxyacid synthase.
    Yoon MY, Gedi V, Kim J, Park Y, Kim DE, Park EH, Choi JD.
    Biochimie; 2010 Jan 10; 92(1):65-70. PubMed ID: 19825392
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