@article { ISI:000323584400008,
	title = {Structural modelling of substrate binding and inhibition in penicillin V acylase from pectobacterium atrosepticum},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {437},
	number = {4},
	year = {2013},
	month = {AUG},
	pages = {538-543},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Penicillin V acylases (PVAs) and bile salt hydrolases (BSHs) have considerable sequence and structural similarity; however, they vary significantly in their substrate specificity. We have identified a PVA from a Gram-negative organism, Pectobacterium atrosepticum (PaPVA) that turned out to be a remote homolog of the PVAs and BSHs reported earlier. Even though the active site residues were conserved in PaPVA it showed high specificity towards penV and interestingly the penV acylase activity was inhibited by bile salts. Comparative modelling and docking studies were carried out to understand the structural differences of the binding site that confer this characteristic property. We show that PaPVA exhibits significant differences in structure, which are in contrast to those of known PVAs and such enzymes from Gram-negative bacteria require further investigation. (C) 2013 Elsevier Inc. All rights reserved.</p>},
	keywords = {Bile salt hydrolase, docking, Homology modelling, Inhibition, Pectobacterium, Penicillin acylase},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2013.06.109},
	author = {Avinash, Vellore Sunder and Panigrahi, Priyabrata and Suresh, C. G. and Pundle, Archana V. and Ramasamy, Sureshkumar}
}
@article {46401,
	title = {Allostery mapping in enterococcus faecalis Bile Salt Hydrolase (BSH)},
	journal = {Acta Crystallographica A-Foundation and Advances},
	volume = {70},
	year = {2014},
	month = {MAY},
	pages = {C274},
	type = {Meeting Abstract},
	keywords = {Allostery, Bile salt hydrolase, MD Simulation},
	issn = {2053-2733},
	author = {Yadav, Yashpal and Ramasamy, Sureshkumar}
}
@article {46378,
	title = {Structure of highly active BSH enzyme with subordinated post-translational excision},
	journal = {Acta Crystallographica A-Foundation and Advances},
	volume = {70},
	year = {2014},
	month = {MAR},
	pages = {C272},
	type = {Meeting Abstract},
	keywords = {Bile salt hydrolase, Mutagenesis, X-ray crystallography},
	issn = {2053-2733},
	author = {Chand, Deepak and Panigrahi, Priyabrata and Ramasamy, Sureshkumar and Suresh, C. G.}
}
@article { ISI:000370100200012,
	title = {Highly active bile salt hydrolase from enterococcus faecalis shows positive cooperative kinetics},
	journal = {Process Biochemistry},
	volume = {51},
	number = {2},
	year = {2016},
	month = {FEB},
	pages = {263-269},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<p>Bile salt hydrolase (BSH; cholylglycine hydrolase, EC 3.5.1.24) is an important enzyme that catalyses the deconjugation of bile acids conjugated with glycine or taurine and assists in the reduction of blood cholesterol levels. In the present study, we report the cloning, overexpression and characterisation of BSH gene from a gut-associated microbe Enterococcus faecalis (EfBSH). The overexpressed protein in Escherichia coli was purified to homogeneity. Optimum pH and temperature for activity were found to be 5.0 and 50 degrees C, respectively. The enzyme was considerably stable in the pH range of 5.0-7.0 and at a temperature of up to 50 degrees C. It showed high specific activity of 1390 U mg(-1) and 1289 U mg-1 for substrates such as glycocholic acid (GCA) and glycodeoxycholic acid (GDCA), respectively. The effect of additives on enzyme activity was assessed, and the detergent Triton X showed a marginally enhanced activity. The enzyme demonstrated unique enzyme kinetics of non-linear regression, thereby displaying positive cooperativity. In addition, the modulating effect of the non-substrate ligand Pen V on the hydrolysing ability of EfBSH towards bile acid such as GDCA was measured. It was observed that Pen V significantly enhanced the BSH activity. This is markedly different from the previously reported competitive inhibition of BSH activity by Pen V. (C) 2015 Elsevier Ltd. All rights reserved.</p>},
	keywords = {Allosteric regulation, Bile acids, Bile salt hydrolase, Enzyme kinetics, Gut organism, Penicillin V acylase},
	issn = {1359-5113},
	doi = {10.1016/j.procbio.2015.12.006},
	author = {Chand, Deepak and Ramasamy, Sureshkumar and Suresh, C. G.}
}
