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OJB©
Online Journal of Bioinformatics©
Volume
5 : 129-131, 2004
In silico gene identification
and homology modeling of Chorismate synthase in Clostridium difficile
Sunita T, Ramadevi S
Informatics Division, GVK BIOSCIENCES Pvt
Ltd,
Sunita T, Ramadevi S In silico gene
identification and homology modeling of Chorismate synthase in Clostridium difficile
Online J Bioinformatics 5 :129-131, 2004. Chorismate synthase
(EC 4.2.3.5), catalyzes the last step in the common shikimate
pathway leading to aromatic compounds. The shikimate
pathway is absent in animals but present in bacteria, fungi, algae and
parasites. Chorismate synthase is a potential therapeutic target for the rational
design of novel antibacterials, antifungals,
antiprotozoals, and herbicides. Herein is described
the identification of gene for chorismate synthase in unfinished genome of Clostridium difficile, a gram positive
bacteria involved in colitis and diarrhea. The predicted protein sequence has
three conserved signature patterns from regions
rich in basic residues (mostly arginines) present in chorismate synthase of various
species. Homology modeling studies based on the crystal structure of chorismate synthase from Helicobacter pylori showed the
conserved FMN binding site with two invariant histidine
residues conserved in the active site : His(17) and His(106). The homology
model described herein should provide a
structural framework on which the design of specific inhibitors may be based.
Keywords: aroC; chorismate synthase; FMN-binding
protein; Clostridium difficile; shikimate
pathway