ChemNet
 
Previous article Next article Contents  

M. G. Khrenova, S. A. Zavyalova, E. Y. Bezsudnova

Molecular mechanism of stereospecificity of transaminase from Desulfohalobium retbaense to D-leucine revealed by molecular dynamics modeling

Abstract

The paper presents the results of a molecular dynamics study of the molecular mechanism of experimentally observed specificity of transaminase from Desulfohalobium retbaense (Dret) to the D-isomer of leucine. A full-atom 3D model of Dret is constructed based on the primary sequence and crystal structures of related enzymes. Analysis of molecular dynamics trajectories demonstrated that the α-COO-group of D-leucine forms stable hydrogen bonds with the Arg54* in the enzyme-substrate complex, that contributes to the proper orientation of the substrate in the active site. The formation of such complex with the L-isomer of leucine leads to the destruction of these hydrogen bonds and disruption of the structure of the entire active site.
Key words: molecular modeling, molecular dynamics, stereospecificity, D-amino-acid transaminase.
Moscow University Chemistry Bulletin.
2020, Vol. 61, No. 3, P. 208
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
   Overview
   Editorial board
   Tables of Contents
   Subscription

The site is supported by Russian Foundation for Basic Research
  The using of published on this page materials is not allowed without special permission
Copyright (C) Chemisty Department of Moscow State University
Web-Editor: B.I.Pokrovskii
Web-design: Copyright (C) MIG and VVM
webmaster@www.chem.msu.su