@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:000316859400002,
	title = {Crystal structure and fluorescence analysis of alkaline thermostable xylanase from bacillus sp (NCL 87-6-10)},
	journal = {Protein and Peptide Letters},
	volume = {20},
	number = {2},
	year = {2013},
	month = {FEB},
	pages = {125-132},
	publisher = {BENTHAM SCIENCE PUBL LTD},
	address = {EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES},
	abstract = {<p>Structural information deduced from the new crystal form of xylanase from Bacillus sp (NCL 87-6-10) (ATBXYL-C) helped us to identify the active site and interpret the stability of the enzyme. The analysis of the tetragonal crystal structure of ATBXYL-C with a bound and cleaved xylotriose revealed the two glutamic acid residues in the structure that could act as nucleophile (Glu94) and base (Glu184) in the enzyme activity and also the tryptophan residues interacting with the substrate. The cleavage of xylotriose in the crystal showed xylobiose to be the major product. Intrinsic fluorescence of the enzyme showed the presence of tryptophans in partially exposed to the solvent at the active site and surface tryptophans in electropositive environment. The titration experiments with xylobiose and xylotriose revealed slightly enhanced preference for longer chain X3 compared with X2. The crystal structure also account for some of the factors, such as increased number of ionic interactions and additional interactions at the N-terminus, which contributed to increased alkalophilicity and thermostability of the enzyme.</p>},
	keywords = {active site residues, Alkaline thermophile Bacillus xylanase (ATBXYL-C), fluorescence studies, three-dimensional structure},
	issn = {0929-8665},
	doi = {10.2174/092986613804725271},
	author = {Satyanarayana, L. and Gaikwad, Sushama M. and Balkrishnan, H. and Suresh, C. G.}
}
