@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 { ISI:000362964900007,
	title = {Sequence and structure-based comparative analysis to assess, identify and improve the thermostability of penicillin G acylases},
	journal = {Journal of Industrial Microbiology \& Biotechnology},
	volume = {42},
	number = {11},
	year = {2015},
	month = {NOV},
	pages = {1493-1506},
	publisher = {SPRINGER HEIDELBERG},
	address = {TIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANY},
	abstract = {<p>Penicillin acylases are enzymes employed by the pharmaceutical industry for the manufacture of semi-synthetic penicillins. There is a continuous demand for thermostable and alkalophilic enzymes in such applications. We have carried out a computational analysis of known penicillin G acylases (PGAs) in terms of their thermostable nature using various protein-stabilizing factors. While the presence of disulfide bridges was considered initially to screen putative thermostable PGAs from the database, various other factors such as high arginine to lysine ratio, less content of thermolabile amino acids, presence of proline in beta-turns, more number of ion-pair and other non-bonded interactions were also considered for comparison. A modified consensus approach designed could further identify stabilizing residue positions by site-specific comparison between mesostable and thermostable PGAs. A most likely thermostable enzyme identified from the analysis was PGA from Paracoccus denitrificans (PdPGA). This was cloned, expressed and tested for its thermostable nature using biochemical and biophysical experiments. The consensus site-specific sequence-based approach predicted PdPGA to be more thermostable than Escherichia coli PGA, but not as thermostable as the PGA from Achromobacter xylosoxidans. Experimental data showed that PdPGA was comparatively less thermostable than Achromobacter xylosoxidans PGA, although thermostability factors favored a much higher stability. Despite being mesostable, PdPGA being active and stable at alkaline pH is an advantage. Finally, several residue positions could be identified in PdPGA, which upon mutation selectively could improve the thermostability of the enzyme.</p>},
	keywords = {Alkalistable, beta-lactam antibiotics, Consensus approach, Disulfide bridge, Ion pairs, Penicillin acylase, Thermostability},
	issn = {1367-5435},
	doi = {10.1007/s10295-015-1690-x},
	author = {Panigrahi, Priyabrata and Chand, Deepak and Mukherji, Ruchira and Ramasamy, Sureshkumar and Suresh, C. G.}
}
