Brownian dynamics simulations of enzyme-enzyme interactions and ligand transfer

PHYS 353

Neville Y. Forlemu, neville.forlemu@und.edu1, Victor F. Waingeh, victor.waingeh@und.nodak.edu2, Eric Njankwa Njabon3, Kristine L. Carlson, kristine.carlson@und.nodak.edu1, and Kathryn A. Thomasson, kthomasson@chem.und.edu3. (1) Chemistry, University of North Dakota, Grand Forks, ND 58202-9024, (2) Department of Chemistry, Eastern Illinois University, 600 Lincoln Ave, Charleston, IL 61920, (3) Department of Chemistry, University of North Dakota, Grand Forks, ND 58202-9024
Functional protein-protein interactions are essential for many physiological processes. Some of these functional interactions have been hypothesized to play a role in substrate channeling and compartmentation. BD agrees with experiments that several glycolytic enzymes interact with F-actin to provide a platform for compartmentation. Herein, the interactions between the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with lactate dehydrogenase (LDH) and fructose-1,6-bisphosphate aldolase (ALD) with GAPDH are also explored to examine potential channeling pathways. Enzyme-enzyme complexes between GAPDH and LDH involve three different binding modes that make use of mainly positively charged lysine residues and negatively charged glutamates and aspartates on both GAPDH and LDH. BD simulations show higher transfer efficiencies of the substrate glyceraldehyde-3-phosphate (GAP) from an aldolase active site to a GAPDH active site as compared to transfer efficiencies of GAP from solution. Similarly. BD simulations suggest a possibility of channeling the cofactor NAD(H) between the GAPDH and LDH.
 

PHYS Poster Session - Multiscale Modeling in Biophysics
7:30 PM-10:00 PM, Wednesday, April 9, 2008 Morial Convention Center -- Hall A, Poster

Division of Physical Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008