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Title

Evolutionary and functional analysis of fructose bisphosphate aldolase of plant parasitic nematodes 

 

Authors

CVS Siva Prasad*, Saurabh Gupta, Himansu Kumar & Murlidhar Tiwari

 

Affiliation

Division of Applied Sciences & IRCB, Indian Institute of Information Technology, Deoghat, Jhalwa, Allahabad 211012, India.

 

Email

shiva@iiita.ac.in; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received November 12, 2012; Accepted November 14, 2012; Published January 09, 2013

 

Abstract

The essential and ubiquitous enzyme fructose bisphosphate aldolase (FBPA) has been a good target for controlling the various types of infections caused by pathogens and parasites. The parasitic infections of nematodes are the major concern of scientific community, leading to biochemical characterization of this enzyme. In this work we have developed a small dataset of all types of FBPA sequences collected from publically available databases (EMBL, NCBI and Uni-Port). The Phylogenetic study shows that evolutionary relationships among sequences of FBPA are clustered into three main groups. FBPA sequences of Globodera rostochiensis (FBPA_GR) and Heterodera glycines (FBPA_HG) are placed in group II, sharing the similar evolutionary relationship. The catalytic mechanism of these enzymes depends upon which class of aldolase, it belongs. The class of enzyme has been confirmed on the basis of sequences and structural similarity with template structure of class I FBPA. To confirm catalytic mechanism of above said model structures, the known substrate fructose-1, 6-bisphosphate (FBP) and competitive inhibitor Mannitol-1, 6 bisphosphate (MBP) were docked at known catalytic site of enzyme of interest. The comparative docking analysis shows that enzyme-substrate complex is forming similar Schiff base intermediate and conducts C3C4 bond cleavage by forming Hydrogen bonding with reaction catalyzing Glu-191, reactive Lys-150, and Schiff base forming Lys-233. On the other hand enzyme-inhibitor noncovalent complex is forming cabinolamine precursor and the proton transfer by the formation of hydrogen bond between MBP O2 with Glu191 enabling stabilization of cabinolamine transition state, which confirms the similar inhibition mechanism. Thus we conclude that Plant Parasitic Nematodes (PPNs) have evolutionary and functional relationship with the class I aldolase enzyme. Hence, FBPA can be targeted to control plant parasitic nematodes.

 

Keywords

FBPA, FBPA_HG, 1ZAH_A, FBP, MBP, PPNs, Modeling, Simulation & Docking.

 

Citation

Prasad et al. Bioinformation 9(1): 001-008 (2013)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.