Abstracts Keynote & Plenary

Genomics, 2006, 7:100.
[2] KJ Kauffman, P Prakash, JS Edwards. Advances in flux balance analysis. Current Opinion in
Biotechnology, 2003, 14:491–496.
PO-041
Class I Phospho-inositide-3-kinases
(PI3Ks) Isoform-specific Inhibition Study by the
Combination of Docking and Molecular Dynamics Simulation
Han, Ming
PO-042
Molecular Dynamics Simulation studies on structural changes and catalytic mechanism of T1
lipase at different temperatures
-Qing Wei 3
Ying Wang ,*
1
, Jing-Fang Wang 2
,*,Dong
1
Department of Bioinformatics and Biostatistics, College of Life Science and Biotechnology, Shanghai
Jiaotong University, Shanghai 200240, China
2
Bioinformatics Center, Key Laboratory of Systems
Biology, Shanghai Institutes for Biological
Sciences, Chinese Academy of Sciences, Shanghai 200031, China
Molecular Dynamics (MD) simulations of T1 lipase movements have revealed the structural
aspects of the T1 lipase responsible for varying activity at different temperature and domain
movements responsible for activity. An interesting structure of T1 lipase was found by using the
long time‐scale molecular dynamics simulations. Overall, the whole T1 lipase molecular was cut
into eight regions in charge of divers functions by the centralβ‐sheet consisting of seven strands
which showed higher stability and constructed the main structure. The active site was
surrounded or covered by the regions which liked petals opening or closing during
temperature‐induced simulations. The active site was on the region 3which was relatively stable.
However, region 2 was accompanied by a large flexibility and dynamics under varying
temperature conditions, so this region was temperature receptor of the T1 lipase. Our studies
explained that T1 lipase had high catalytic activity at 70℃, because exposure time of the active
site was long and the size of the pocket was comfortable. In addition, at lower or higher
temperature, the structure of T1 lipase played great changes and the surface area exposed to
solvent was too large, thus the activity was lost. All these findings might provide significant
evidence for the catalytic mechanism of T1 lipase.