@article { ISI:000245519000057,
	title = {Tryptophan residue is identified in the substrate binding of penicillin G acylase from Kluyvera citrophila},
	journal = {Enzyme and Microbial Technology},
	volume = {40},
	number = {5},
	year = {2007},
	month = {APR},
	pages = {1389-1397},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Penicillin acylases are important enzymes in pharmaceutical industry for the production of semi-synthetic beta-lactam antibiotics via the key intermediate 6-aminopenicillanic acid. The penicillin G acylase purified from Kluyvera citrophila (KcPGA) on modification with tryptophan-specific reagents such as N-bromo succinamide (NBS) and 2-hydroxy 5-nitrobenzylbromide (HNBB) showed partial loss of activity and substrate protection. Various solute quenchers and substrate were used to probe the microenvironment of the putative reactive tryptophan through fluorescence quenching. Homology modeling of KcPGA structure has been carried out. Docking substrate on this modeled KcPGA structure identifies the tryptophan residue that is directly influenced by substrate binding. To confirm the biological significance of this particular tryptophan, we did a sequence comparison of PGAs from various organisms. The sequence alignment clustered the matches into two sets, those closer to (\&gt; 40\% identical) KcPGA and had the tryptophan of interest present in them formed the first set, while those less identical (\&lt; 30\%) to KcPGA and the particular tryptophan absent in them formed the second set. It is clear from the reported kinetic parameters of representative members of these two sets that the affinity for penicillin G (penG) of the former class is several times better. Thus, based on our studies we suggest that the tryptophan residue in the identified position is important for binding substrate penG by the acylases. (c) 2006 Elsevier Inc. All rights reserved.</p>},
	keywords = {fluorescence measurement, K. citrophila, Penicillin G acylase, sequence alignment, substrate-docking, tryptophan modification},
	issn = {0141-0229},
	doi = {10.1016/j.enzmictec.2006.10.022},
	author = {Kumar, R. Suresh and Prabhune, Asmita and Pundle, A. V. and Karthikeyan, Muthukumarasamy and Suresh, C. G.}
}
@article { ISI:000360934400007,
	title = {Design and development of cheminfocloud: an integrated cloud enabled platform for virtual screening},
	journal = {Combinatorial Chemistry \& High Throughput Screening},
	volume = {18},
	number = {6},
	year = {2015},
	month = {JAN},
	pages = {604-619},
	publisher = {BENTHAM SCIENCE PUBL LTD},
	address = {EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES},
	abstract = {<p>The power of cloud computing and distributed computing has been harnessed to handle vast and heterogeneous data required to be processed in any virtual screening protocol. A cloud computing platorm ChemInfoCloud was built and integrated with several chemoinformatics and bioinformatics tools. The robust engine performs the core chemoinformatics tasks of lead generation, lead optimisation and property prediction in a fast and efficient manner. It has also been provided with some of the bioinformatics functionalities including sequence alignment, active site pose prediction and protein ligand docking. Text mining, NMR chemical shift (1H, 13C) prediction and reaction fingerprint generation modules for efficient lead discovery are also implemented in this platform. We have developed an integrated problem solving cloud environment for virtual screening studies that also provides workflow management, better usability and interaction with end users using container based virtualization, OpenVz.</p>},
	keywords = {Chemoinformatics, cloud computing, machine learning, Molecular docking, OpenVz, sequence alignment, spectra prediction, text mining, virtual screening},
	issn = {1386-2073},
	doi = {10.2174/1386207318666150703113656},
	author = {Karthikeyan, Muthukumarasamy and Pandit, Deepak and Bhavasar, Arvind and Vyas, Renu}
}
