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OJB

 

Online Journal of Bioinformatics

Volume 7 (1) : 35-45, 2006.


Comparative structure analysis of chorismate synthase. 

 

Marla S , Yalamanchili HK,  Gelli P, Singh HK, Praveen G, Ghatta G, Srikanth S, Goutham K.

 

Biotechnology and Bioinformatics Department, JayaPrakash University of Information technology, Solan, H.P.173215, India.

 

ABSTRACT

 

Marla S , Yalamanchili HK,  Gelli P, Singh HK, Praveen G, Ghatta G, Srikanth S, Goutham K, Comparative structure analysis of Chorismate synthase, Onl J Bioinform., 7 (1) : 35 - 45, 2006. This work compares chorismate synthase structure in various microorganisms. The enzyme is essential in the shikomate pathway  in  bacteria, fungi and plants, but not in mammals. It is a useful target for drug design inhibiting functional pathways with chemotherapeutic effects. Binding of essential co-factors Flavin mononucleotide (FMN) and 5-enolpyruvil shikomate-3-phosphate(EPSP) affects its activity. The results of FMN structure analysis and in various microorganisms are presented. Comparative modeling  and extent of structure similarities between  H. pyroli and P. rumnicola were performed using alpha and beta fold patterns, FMN binding and main chain configuration residues. Active sites for binding of  FMN were detected.  Phylogeny analysis was evaluated in various microorganisms.

 

Key words: Chorismate synthase, flavin mononucleotide, Binding sites, Helicobacter pyroli, Prevotella rumnicola.


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