1 March 2005 Computational Investigations of the Octameric Enolase Enzyme
Debra L. Bautista, Wesley Penn, Karen Simonetti
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Each step of glycolysis is characterized by a specific enzyme that acts to catalyze a given reaction. Unique amongst these reactions is the enolase-catalyzed transformation of 2-phosphoglycerate into phosphoenolpyruvate by dehydration. Studies have shown enolase to have a dimeric structure in all eukaryotes whereas the enzyme has been observed to possess an octameric structure in some extreme thermophile prokaryotes. Though a definitive determination of molecular architecture has not been made, anecdotal evidence seems to indicate that a tetrameric association of dimers is the most likely native form. This study has produced computational models for three mutation/deletion variants of the enzyme HL–S1 loop, which has been proposed as a contact point between the dimer subunits. Examination of these models with a dielectric constant of 40 has indicated a rapid deterioration of protein conformation; however, dielectric constants of 0 and 80 maintained overall structure. The study also showed that the deletion of residues 135–138 did not completely eliminate the alpha helix that was hypothesized to inhibit octameric structure.

Debra L. Bautista, Wesley Penn, and Karen Simonetti "Computational Investigations of the Octameric Enolase Enzyme," Journal of the Kentucky Academy of Science 66(1), 17-23, (1 March 2005). https://doi.org/10.3101/1098-7096(2005)66[17:CIOTOE]2.0.CO;2
Published: 1 March 2005
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