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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Detalles Bibliográficos
Autores principales: 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.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
Ligands That Aid in Function Characterization
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954222/
https://www.ncbi.nlm.nih.gov/pubmed/20944228
http://dx.doi.org/10.1107/S1744309110021688

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954222/
https://www.ncbi.nlm.nih.gov/pubmed/20944228
http://dx.doi.org/10.1107/S1744309110021688

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