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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, Hyderabad, India
Sunita T, Ramadevi
S In silico gene identification and homology modeling of Chorismate
synthase in Clostridium difficile Onl J Bioinform., 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