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OJBTM
Online Journal of Bioinformatics ©
Volume
12(2):413-430, 2011.
In Silico substrate specificity in bmgt1 and bmgt2 genes of Bacopa monniera
glycosyltransferases.
Sharma R, Ruby Zargar, Khan BM, Suresh CG.
Division
of Biochemical Sciences and Plant Tissue Culture Division, National Chemical
Laboratory, Pune, India
ABSTRACT
Sharma R, Ruby Z, Khan BM, Suresh CG.,
In Silico substrate specificity in bmgt1 and bmgt2 genes of Bacopa
monniera glycosyltransferases, Onl
J Bioinform., 12(2):413-430, 2011.
Sequence analysis, structure prediction and docking for glycosyltransferases
coded by the bacopa
monnieri genes bmgt1 and
bmgt2 is
described. Molecular structures were modeled by comparative modeling
and energy minimization. Bmgt1 had secondary structure elements 12
á-helices and 10 â-sheets and bmgt2, 15 á-helices and 12
â-sheets. The root mean square deviation (RMSD) between modeled
structures and corresponding templates was ~1 Å. Docking studies using
various acceptor and donor molecules have shown that the structurally conserved
Cterminal domain binds the donor molecule and the
highly variable N-terminal domain, which can accept a range of molecules, binds
the acceptor molecule. The differences between the structures of bmgt1 and
bmgt2, their specificities and interactions with various ligands were analyzed.
A histidine in the N-terminal domain, conserved throughout the GT families, is
a key residue that interacts with the acceptor molecule. Several residues of
the highly conserved motif called “plant secondary product glycosyltransferse
(PSPG)” that interact with the donor molecule might determine the specificity
of enzyme for particular sugar donor. Modeling studies show that a Trp in bmgt1 and Arg in the same
position of bmgt2 of PSPG motif may play a role in deciding the sugar
specificity of these two enzymes.
Keywords: Docking; Energy minimization; Glycosyltransferase;
UDP-Glucose; UDP-Glucuronic acid; Wide specificity
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