@article {1223,
	title = {Letter to the editor: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation},
	journal = {Journal of Biomolecular Nmr},
	volume = {31},
	number = {4},
	year = {2005},
	note = {ISI Document Delivery No.: 931SKTimes Cited: 1Cited Reference Count: 7},
	month = {Apr},
	pages = {371-372},
	type = {Article},
	keywords = {auto-proteolysis, DYNAMICS, LexA, N-15 NMR RELAXATION, NMR ASSIGNMENTS, PROTEIN, SOS response},
	isbn = {0925-2738},
	url = {<Go to ISI>://000229505400016},
	author = {Okon, M. and Pfuetzner, R. and Vuckovic, M. and Little, J. W. and Strynadka, N. C. J. and McIntosh, L. P.}
}
@article {713,
	title = {Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens},
	journal = {Carbohydrate Research},
	volume = {338},
	number = {5},
	year = {2003},
	note = {ISI Document Delivery No.: 645XBTimes Cited: 6Cited Reference Count: 38},
	month = {Feb},
	pages = {415-421},
	type = {Article},
	abstract = {The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate omicron-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pK(a) values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an similar to 10-fold higher k(cat)/K-m value with this substrate at pH 6 and 40 degreesC, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. (C) 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {bacillus xylanase, CIRCULANS XYLANASE, CLASSIFICATION, electrostatic, extremophile, glycosidase, GLYCOSYL-ENZYME INTERMEDIATE, HYDROLASES, interactions, NMR ASSIGNMENTS, pH-dependent mechanism, PK(A), PROTEIN, STABILITY, THERMOSTABILITY},
	isbn = {0008-6215},
	url = {<Go to ISI>://000181004800004},
	author = {Poon, D. K. Y. and Webster, P. and Withers, S. G. and McIntosh, L. P.}
}
@article {4020,
	title = {Complete measurement of the pK(a) values of the carboxyl and imidazole groups in Bacillus circulans xylanase},
	journal = {Protein Science},
	volume = {6},
	number = {12},
	year = {1997},
	note = {ISI Document Delivery No.: YK912Times Cited: 44Cited Reference Count: 29},
	month = {Dec},
	pages = {2667-2670},
	type = {Article},
	abstract = {Electrostatic interactions in proteins can be dissected experimentally by determining the pK(a), values of their constituent ionizable amino acids. To complement previous studies of the glutamic acid and histidine residues in Bacillus circulans xylanase (BCX), we have used NMR methods to measure the pK(a)s of the seven aspartic acids and the C-terminus of this protein. The pK(a)s of these carboxyls are all less than the corresponding values observed with random coil polypeptides, indicating that their ionization contributes favorably to the stability of the folded enzyme. In general, the aspartic acids with the most reduced pK(a)s are those with limited exposure to the solvent and a high degree of conservation among homologous xylanases. Most dramatically, Asp 53 and Asp 101 have pK(a)s < 2 and thus remain deprotonated in native BCX under all conditions examined. Asp 83 is completely buried, forming a strong salt bridge with Arg 136. In contrast, Asp 101 is located on the surface of the protein, stabilized in the deprotonated form by an extensive network of hydrogen bonds involving an internal water molecule and the neutral side-chain and main-chain atoms of Ser 100 and Thr 145. These data provide a complete experimental database for theoretical studies of the ionization behavior of BCX under acidic conditions.},
	keywords = {aspartic acid, electrostatics, FAMILIES, NMR, NMR ASSIGNMENTS, NUCLEAR-MAGNETIC-RESONANCE, PK(A), PROTEINS, RESIDUES, SHIFTS, titration, XYLANASE},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1997YK91200024},
	author = {Joshi, M. D. and Hedberg, A. and McIntosh, L. P.}
}
