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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Main 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-André, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A., Wilson, Ian A.
Format: Artigo
Jezik:Inglês
Izdano: International Union of Crystallography 2010
Teme:
Ligands That Aid in Function Characterization
Online dostop: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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