@article { ISI:000359166300001,
	title = {Penicillin V acylase from pectobacterium atrosepticum exhibits high specific activity and unique kinetics},
	journal = {International Journal of Biological Macromolecules},
	volume = {79},
	year = {2015},
	month = {AUG},
	pages = {1-7},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Penicillin V acylases (PVAs, E.C.3.5.11) belong to the Ntn hydrolase super family of enzymes that catalyze the deacylation of the side chain from phenoxymethyl penicillin (penicillin V). Penicillin acylases find use in the pharmaceutical industry for the production of semi-synthetic antibiotics. PVAs employ the N-terminal cysteine residue as catalytic nucleophile and are structurally and evolutionarily related to bile salt hydrolases (BSHs). Here, we report the cloning and characterization of a PVA enzyme from the Gram-negative plant pathogen, Pectobacterium atrosepticum (PaPVA). The enzyme was cloned and expressed in Escherichia coli attaining a very high yield (250 mg/l) and a comparatively high specific activity (430 IU/mg). The enzyme showed marginally better pH and thermo-stability over PVAs characterized from Gram-positive bacteria. The enzyme also showed enhanced activity in presence of organic solvents and detergents. The enzyme kinetics turned out to be significantly different from that of previously reported PVAs, displaying positive cooperativity and substrate inhibition. The presence of bile salts had a modulating effect on PaPVA activity. Sequence analysis and characterization reveal the distinctive nature of these enzymes and underscore the need to study PVAs from Gram-negative bacteria. (C) 2015 Elsevier B.V. All rights reserved.</p>},
	keywords = {Cooperative, Enzyme kinetics, Gram-negative, Penicillin V acylase, Substrate inhibition},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2015.04.036},
	author = {Avinash, Vellore Sunder and Ramasamy, Sureshkumar and Suresh, C. G. and Pundle, Archana}
}
