@article { ISI:000257961500018,
	title = {Isolation and heterologous expression of PHA synthesising genes from Bacillus thuringiensis R1},
	journal = {World Journal of Microbiology \& Biotechnology},
	volume = {24},
	number = {9},
	year = {2008},
	month = {SEP},
	pages = {1769-1774},
	publisher = {SPRINGER},
	type = {Article},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>The polyhydroxyalkanoate biosynthesis gene locus from Bacillus thuringiensis R1 was isolated, cloned and analyzed at the molecular level. We found that a similar to 5 kb SacI-ClaI digested fragment of genomic DNA from B. thuringiensis R1 encoding the PHA synthesising genes, conferred PHA producing ability to E. coli. The fragment was sequenced and found to be of 4787 bp with five open reading frames. Sequence alignment with closely related species of Bacillus in the existing database revealed that the ORFs correspond to phaP, phaQ, phaR, phaB and phaC genes. However, E. coli harboring phaP, phaQ, phaR, phaB and phaC locus produced very low PHA. Furthermore, complementation of the locus with phaA from Ralstonia eutropha increased the PHA production in the recombinant E. coli from 3.0\% to 24\% of cell dry mass. The putative promoter regions and ribosome binding sites were identified for each of the gene. Conserved domains for PHA synthase and aceto-acetyl-coA reductase were also identified. We hence conclude that the PHA operon of Bacillus thuringiensis R1 consists of phaP, phaQ, phaR, phaB, phaC and complementation of the same with phaA is accountable for its high PHA production.</p>},
	keywords = {aceto-acetyl-coA reductase, Bacillus thuringiensis R1, PHA synthase, polyhydroxyalkanoate},
	issn = {0959-3993},
	doi = {10.1007/s11274-008-9669-7},
	author = {Desetty, Rohini D. and Mahajan, Vineet S. and Khan, Bashir Mohammad and Rawal, Shuban K.}
}
@article { ISI:000357458400018,
	title = {In silico ligand binding studies of cyanogenic beta-glucosidase, dhurrinase-2 from Sorghum bicolor},
	journal = {Journal of Molecular Modeling},
	volume = {21},
	number = {7},
	year = {2015},
	month = {JUL},
	pages = {184},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Dhurrinase, a cyanogenic beta-glucosidase from Sorghum bicolor is the key enzyme responsible for the hydrolysis of dhurrin to produce toxic hydrogen cyanide, as a part of plant defence mechanism. Dhurrinase 1 (SbDhr1) and dhurrinase 2 (SbDhr2), two isozymes have been isolated and characterized from S. bicolor. However, there is no information in the literature about the three dimensional (3D) structure of SbDhr2 and molecular interactions involved between the protein and ligand. In this study, the three dimensional structure of SbDhr2 was built based on homology modeling by using the X-ray crystallographic structure of its close homologue SbDhr1 as the template. The generated 3D model was energy minimized and the quality was validated by Ramachndran plot, various bioinformatic tools and their relevant parameters. Stability, folding-unfolding and flexibility of the modeled SbDhr2 was evaluated on the basis of RMSD, radius of gyration (R-g) and RMSF values respectively, obtained through molecular dynamic (MD) simulation. Further, molecular docking was performed with its natural substrate dhurrin, one substrate analogue, three un-natural substrates, and one inhibitor. Analysis of molecular interactions in the SbDhr2-ligand complexes revealed the key amino acid residues responsible to stabilize the ligands within the binding pocket through non-bonded interactions and some of them were found to be conserved (Glu239, Tyr381, Trp426, Glu454, Trp511). Reasonably broader substrate specificity of SbDhr2 was explained through the wider entrance passage observed in comparison to SbDhr1.</p>},
	keywords = {beta-Glucosidase, Dhurrinase, Molecular docking, Molecular dynamic simulation, Sorghum bicolor},
	issn = {1610-2940},
	doi = {10.1007/s00894-015-2730-1},
	author = {Mahajan, Chavi and Patel, Krunal and Khan, Bashir Mohammad and Rawal, Shuban S.}
}
