Visualization of the Differential Transition State Stabilization within the Active Site Environment

International Journal of Molecular Sciences

Paweł Kᆝzierski¹  Paweł Wielgus¹  Adrian Sikora¹  W. Andrzej Sokalski¹ 

[1] Molecular Modeling Laboratory, Institute of Physical and Theoretical Chemistry, Wroclaw University of Technology, ul. Wyb. Wyspianskiego 27, 50-370 Wroclaw, Poland, tel. [phone], fax [phone]

关键词: Differential Transition State Stabilization;    Catalytic properties;    Visualization;    Enzymatic catalysis;    Molecular electrostatic potential;    Molecular Electrostatic field;    Multipole moments;   

DOI  :  10.3390/i5040186

来源: mdpi

【 摘 要 】

Increasing interest in the enzymatic reaction mechanisms and in the nature of catalytic effects in enzymes causes the need of appropriate visualization methods. A new interactive method to investigate catalytic effects using differential transition state stabilization approach (DTSS) [1,2] is presented. The catalytic properties of the active site of cytidine deaminase (E.C. 3.5.4.5) is visualized in the form of differential electrostatic properties. The visualization was implemented using scripting interface of VMD [3]. Cumulative Atomic Multipole Moments (CAMM) [4,5,6] were utilized for efficient yet accurate evaluation of the electrostatic properties. The implementation is efficient enough for interactive presentation of catalytic effects in the active site of the enzyme due to transition state or substrate movement. This system of visualization of DTTS approach can be potentially used to validate hypotheses regarding the catalytic mechanism or to study binding properties of transition state analogues.

【 授权许可】

Unknown   
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