Gene Cloning and Homology Modeling of the 3-Oxoacyl-ACP Synthase from Aeromonas hydrophila for Drug Discovery

Abstract

Fatty acid biosynthesis in the Aeromonas hydrophila plays an important role in the formation of cell membrane and cell viability. The 3-oxoacyl-acyl carrier protein (ACP) synthase fadH and fadB from A. hydrophila have contributed in the initiation and elongation of fatty acid biosynthesis. In this study, we have designed new set of primers for amplification of the open reading frame of fadH and fadB. Cloning and sequencing of these amplified genes, analyzed that the G+C content of fadH and fadB were 63.3% and 68.79% respectively. The homology modeling was performed to generate the 3-D structure of fadH and fadB; and showed that more than 90% amino acid residues in allowed region of Ramachandranan plot. These findings provide a new avenue for better understanding, the role of genes encoding proteins involved in the fatty acid biosynthesis and thereby using as a potential and novel target for structure based drug designing to control the infections of A. hydrophila.

Analysis of the multicopper oxidase gene regulatory network of Aeromonas hydrophila

“…MCO protein sequence of A. hydrophila was used to generate 3-D structure using known crystal 3-D structure (1KV7). There are recent reports available on homology modeling for generation of 3-D structures of adenosine A2a receptor of Homo sapiens (Singh and Somvanshi 2009a), 3-oxoacyl-acyl carrier protein synthase II of Mycobacterium tuberculosis H37Rv (Singh and Somvanshi 2009b) proteins of A. hydrophila such as aerolysin (Singh and Somvanshi 2009c), hemolysin (Singh et al 2009) and 3-oxoacyl-ACP synthase (Singh et al 2011a). It contains a-helix which involves regularly spaced H-bonds between residues along a chain while b-sheets involves H-bonding between the backbone residues in adjacent chains.…”

“…In the Clade C bacteria may play the similar role in biodegradation of aromatic and phenolic compounds that includes Sulfonaphthal, Thymolphthalein, Bromocresol green and Phloretin. Thus, there are other proteins such as hemolysin (Singh et al 2009), aerolysin (Singh and Somvanshi 2009c), thermostable hemolysin (Singh et al 2011b) and fab (Singh et al 2011a) of A. hydrophila have been investigated for evolutionary relationship with other bacteria using phylogenetic analysis. In the Clade C homology of MCO which is present in other bacteria such as Erwinia, Serretia and Yersinia can also be used for biodegradation of aromatic and phenolic compounds.…”