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Biochemistry|June 2, 2004
pH Dependence of the reaction catalyzed by avian mitochondrial phosphoenolpyruvate carboxykinaseTodd Holyoak, Thomas NowakProteins|May 25, 2023
Biochemical, structural, and kinetic characterization of PPi -dependent phosphoenolpyruvate carboxykinase from Propionibacterium freudenreichiiMatthew J McLeod, Todd HolyoakBiochemistry|August 10, 2007
Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acidSarah M Sullivan, Todd HolyoakProceedings of the National Academy of Sciences of the United States of America|September 6, 2008
Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selectionSarah M Sullivan, Todd HolyoakBiochemistry|May 19, 2010
Increasing the conformational entropy of the Omega-loop lid domain in phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic fidelityTroy A Johnson, Todd HolyoakProceedings of the National Academy of Sciences of the United States of America|April 12, 2007
Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2Joshua L Wheatley, Todd HolyoakBiochemistry|November 7, 2012
The Ω-loop lid domain of phosphoenolpyruvate carboxykinase is essential for catalytic functionTroy A Johnson, Todd HolyoakProceedings of the National Academy of Sciences of the United States of America|August 25, 2025
Structure of the Thomasclavelia ramosa immunoglobulin A protease reveals a modular and minimizable architecture distinct from other immunoglobulin A proteasesNorman Tran, Aaron Frenette, Todd HolyoakBiochemistry|July 6, 2006
Structural insights into the mechanism of PEPCK catalysisTodd Holyoak, Sarah M Sullivan, Thomas NowakBiochemistry|December 29, 2015
Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate CarboxykinaseTroy A Johnson, Matthew J Mcleod, Todd HolyoakPageof 5