@article { ISI:000237440200012,
	title = {Structural and active site modification studies implicate Glu, Trp and Arg in the activity of xylanase from alkalophilic Bacillus sp (NCL 87-6-10)},
	journal = {Enzyme and Microbial Technology},
	volume = {39},
	number = {1},
	year = {2006},
	month = {JUN},
	pages = {67-73},
	publisher = {ELSEVIER SCIENCE INC},
	type = {Article},
	address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA},
	abstract = {<p>Structural studies and residue modification using group specific reagents were used to ascertain the role of different functional groups in xylanase from alkalophilic Bacillus sp. (NCL 87-6-10). Treatment with N-bromosuccinimide resulted in fast enzyme inactivation. Reaction with Woodward{\textquoteright}s reagent K resulted in initial fast followed by slower inactivation. In both cases enzyme was protected against inactivation by the substrate, xylan. The reaction of the enzyme with phenylglyoxal has revealed one essential arginine residue at the active site. The three-dimensional structural analysis of the xylanase at 2.8 angstrom resolution also implicates involvement of Trp, and Arg residues and carboxylate groups in the binding of substrate and in the catalysis of xylanase. (c) 2005 Published by Elsevier Inc.</p>},
	keywords = {active-site residues, alkaline xylanase, Chemical modification, three-dimensional structure},
	issn = {0141-0229},
	doi = {10.1016/j.enzmictec.2005.09.010},
	author = {Balakrishnan, H. and Satyanarayana, L. and Gaikwad, S. M. and Suresh, C. G.}
}
@article { ISI:000272134300006,
	title = {Interaction of alpha-mannosidase from aspergillus fischeri with glycosidase inhibitors, metal ions and group specific reagents},
	journal = {Research Journal of Biotechnology},
	volume = {4},
	number = {4},
	year = {2009},
	month = {NOV},
	pages = {39-48},
	publisher = {RESEARCH JOURNAL BIOTECHNOLOGY},
	address = {SECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIA},
	abstract = {<p>As an initial step towards using alpha-mannosidase as a target against anticancer drugs, inhibition studies of a model enzyme, class II alpha-mannosidase from Aspergillus fischeri in presence of polyhydroxy piperidine derived glycosidase inhibitors, metal ions and amino acid specific reagents were carried out to reveal the sensitivity of the enzyme. Three of the derivatives (Compound 20, 32 and 39)(11) showed competitive inhibition (K(i) =45, 48 and 235 mu M) and the binding of the inhibitors to the enzyme was entropically driven. Among the metal ions checked, Cu(++) (K(i) = 21nm) and Se(++) ions (K(i) = 32 mu M) showed noncompetitive and Co(++) (K(i) = 1.195 mM) showed competitive inhibition of the enzyme activity with insignificant change in the secondary structure of the protein. The above studies exhibit the Potential of the enzyme in studying anticancer drugs. Treatment of the enzyme with group specific reagents showed the presence of carboxylate, Arg and Cys at the active site. Substrate protection studies and kinetics of the modified enzyme confirmed the above results. Trp and His at the active site were observed to be in proximity.</p>},
	keywords = {active-site, alpha-Mannosidase, Chemical modification, Glycosidase inhibitors, metal ions},
	issn = {0973-6263},
	author = {Shashidhara, K. S. and Gaikwad, S. M. and Khan, Mohammad Islam and Bharadwaj, Kishor Chandra and Pandey, G.}
}
