Substrate Effect on Catalytic Loop and Global Dynamics of Triosephosphate Isomerase

Substrate Effect on Catalytic Loop and Global Dynamics of Triosephosphate Isomerase

The opening/closure of the catalytic loop 6 over the active site in apo triosephosphate isomerase (TIM) has been previously shown to be driven by the global motions of the enzyme, specifically the counter-clockwise rotation of the subunits. In this work, the effect of the substrate dihydroxyacetone...

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Bibliographic Details
Main Authors: Pemra Doruker, Zeynep Kurkcuoglu
Format: Article
Language:English
Published: MDPI AG 2013-03-01
Series:Entropy
Subjects:
molecular dynamics simulation
essential dynamics
collective motions
functional loop dynamics
triosephosphate isomerase
dihydroxyacetone phosphate
loop closure
Online Access:http://www.mdpi.com/1099-4300/15/3/1085

Internet

http://www.mdpi.com/1099-4300/15/3/1085

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