The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes Article

Chiu, Hsiu-Ju, Abdubek, Polat, Astakhova, Tamara et al. (2010). The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes . ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 66 1317-1325. 10.1107/S1744309110021688

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cited authors

  • Chiu, Hsiu-Ju; Abdubek, Polat; Astakhova, Tamara; Axelrod, Herbert L; Carlton, Dennis; Clayton, Thomas; Das, Debanu; Deller, Marc C; Duan, Lian; Feuerhelm, Julie; Grant, Joanna C; Grzechnik, Anna; Han, Gye Won; Jaroszewski, Lukasz; Jin, Kevin K; Klock, Heath E; Knuth, Mark W; Kozbial, Piotr; Krishna, S Sri; Kumar, Abhinav; Marciano, David; McMullan, Daniel; Miller, Mitchell D; Morse, Andrew T; Nigoghossian, Edward; Okach, Linda; Reyes, Ron; Tien, Henry J; Trame, Christine B; van den Bedem, Henry; Weekes, Dana; Xu, Qingping; Hodgson, Keith O; Wooley, John; Elsliger, Marc-Andre; Deacon, Ashley M; Godzik, Adam; Lesley, Scott A; Wilson, Ian A

sustainable development goals

authors

publication date

  • October 1, 2010

published in

keywords

  • ACT DOMAIN
  • AQUIFEX-AEOLICUS
  • BIOCHEMICAL-CHARACTERIZATION
  • Biochemical Research Methods
  • Biochemistry & Molecular Biology
  • Biophysics
  • CRYSTAL-STRUCTURE
  • CYCLOHEXADIENYL DEHYDROGENASE
  • Crystallography
  • DIFFRACTION DATA
  • ESCHERICHIA-COLI
  • Life Sciences & Biomedicine
  • MUTAGENESIS
  • PROTEIN
  • Physical Sciences
  • Science & Technology
  • TYROSINE

Digital Object Identifier (DOI)

start page

  • 1317

end page

  • 1325

volume

  • 66