@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 {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.}
}
