Rajesh, P. S. and Rai, V. R. (2014) Molecular identification of aiiA homologous gene from endophytic Enterobacter species and in silico analysis of putative tertiary structure of AHL-lactonase. Biochemical and Biophysical Research Communications, 443 (1). pp. 290-295.
Full text not available from this repository. (Request a copy)Abstract
The aiiA homologous gene known to encode AHL- lactonase enzyme which hydrolyze the N-acylhomoserine lactone (AHL) quorum sensing signaling molecules produced by Gram negative bacteria. In this study, the degradation of AHL molecules was determined by cell-free lysate of endophytic Enterobacter species. The percentage of quorum quenching was confirmed and quantified by HPLC method (p\textless 0.0001). Amplification and sequence BLAST analysis showed the presence of aiiA homologous gene in endophytic Enterobacter asburiae VT65, Enterobacter aerogenes VT66 and Enterobacter ludwigii VT70 strains. Sequence alignment analysis revealed the presence of two zinc binding sites, "HXHXDH" motif as well as tyrosine residue at the position 194. Based on known template available at Swiss-Model, putative tertiary structure of AHL-lactonase was constructed. The result showed that novel endophytic strains of Enterobacter genera encode the novel aiiA homologous gene and its structural importance for future study.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | controlled study, nonhuman, tyrosine, bacterial strain, priority journal, computer model, article, high performance liquid chromatography, Phylogeny, Bacterial, Genes, gene identification, Enterobacter, gluconolactonase, n acylhomoserine lactone, quorum sensing, endophyte, Amino Acid Sequence, sequence alignment, Sequence Alignment, Negibacteria, binding site, DNA template, Enterobacter aerogenes, Molecular Sequence Data, Protein Structure, Tertiary, Metalloendopeptidases, Computer Simulation, enzyme conformation, AHL-lactonase, aiiA gene, Carboxylic Ester Hydrolases, cell free system, cell lysate, Enterobacter asburiae, Enterobacter ludwigii, Enterobacter species, enzymatic degradation, Genetic Association Studies, Quorum quenching, Tertiary structure, zinc binding protein |
| Subjects: | B Life Science > Microbiology |
| Divisions: | Department of > Microbiology |
| Depositing User: | Arshiya Kousar Library Assistant |
| Date Deposited: | 28 Aug 2019 06:05 |
| Last Modified: | 28 Aug 2019 06:05 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/4356 |
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