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

Chorismate mutase/prephenate dehydrogenase from Haemophilus influenzae Rd KW20 is a bifunctional enzyme that catalyzes the rearrangement of chorismate to prephenate and the NAD(P)(+)-dependent oxidative decarboxyl­ation of prephenate to 4-hydroxyphenylpyruvate in tyrosine biosynthesis. The crystal s...

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Bibliografiset tiedot
Päätekijät: 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-André, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., Wilson, Ian A.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: International Union of Crystallography 2010
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC2954222/
https://ncbi.nlm.nih.gov/pubmed/20944228
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309110021688
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