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1. Disruption of the proton relay network in the class 2 dihydroorotate dehydrogenase from Escherichia coli

Author

Kow, Rebecca L., Whicher, Jonathan R., Palfey, Bruce A., and Fagan, Rebecca L.

Subjects
Phenylalanine -- Chemical properties, Phenylalanine -- Structure, Serine -- Chemical properties, Serine -- Structure, Threonine -- Chemical properties, Threonine -- Structure, Oxidation-reduction reaction -- Analysis, Escherichia coli -- Research, Hydrogen bonding -- Research, Biological sciences, Chemistry
Abstract

A site-directed mutagenesis study was conducted to explore the significance of residues Ser175, phenylalanine Phe115, and threonine Thr178 in Escherichia coli towards the oxidation of dihydroorotate (DHO). Changing the size and/or hydrophobicity of the residues of the hydrogen bond network, Thr178 and Phe115 which slowed flavin reduction as much as 2 orders of magnitude, indicated that the active site base and the hydrogen bond network work together for efficient deprotonation of DHO.

Published
2009

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