Molecular identification of aiiA homologous gene from endophytic Enterobacter species and in silico analysis of putative tertiary structure of AHL-lactonase

•Novel endophytic Enterobacter species was identified with the presence of aiiA homologous gene.•Multiple Sequence Alignment analysis revealed the presence of two zinc binding sites, "HXHXDH" motif and tyrosine residue.•Based on sequence analysis the putative tertiary structure of AHL-lact...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2014-01, Vol.443 (1), p.290-295
Main Authors: Rajesh, P.S., Rai, V. Ravishankar
Format: Article
Language:English
Subjects:
AHL-lactonase
aiiA gene
Amino Acid Sequence
Carboxylic Ester Hydrolases - chemistry
Carboxylic Ester Hydrolases - classification
Carboxylic Ester Hydrolases - genetics
Computer Simulation
Enterobacter
Enterobacter - enzymology
Enterobacter - genetics
Enterobacter aerogenes
Enterobacter species
Genes, Bacterial
Genetic Association Studies
Metalloendopeptidases - chemistry
Metalloendopeptidases - classification
Metalloendopeptidases - genetics
Molecular Sequence Data
Phylogeny
Protein Structure, Tertiary
Quorum quenching
Sequence Alignment
Tertiary structure
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Summary:•Novel endophytic Enterobacter species was identified with the presence of aiiA homologous gene.•Multiple Sequence Alignment analysis revealed the presence of two zinc binding sites, "HXHXDH" motif and tyrosine residue.•Based on sequence analysis the putative tertiary structure of AHL-lactonase was constructed. 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
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2013.11.101