@article { ISI:000177228000001,
	title = {Mechanism of Thermoanaerobacterium saccharolyticum ss-xylosidase: Kinetic studies},
	journal = {BIOCHEMISTRY},
	volume = {41},
	number = {31},
	year = {2002},
	month = {AUG 6},
	pages = {9727-9735},
	abstract = {{The catalytic mechanism of Thermoanaerobacterium saccharolyticum beta-xylosidase (XynB) from family 39 of glycoside hydrolases has been subjected to a detailed kinetic investigation using a range of substrates. The enzyme exhibits a bell-shaped pH dependence of k(cat)/K(m), reflecting apparent pK(a) values of 4.1 and 6.8. The k(cat) and k(cat)/K(m) values for a series of aryl xylosides have been measured and used to construct two Bronsted plots. The plot of log(k(cat)/K(m)) against the pK(a) of the leaving group reveals a significant correlation (beta(1g) = -0.97, r(2) = 0.94},
	issn = {0006-2960},
	doi = {10.1021/bi020077v},
	author = {Vocadlo, DJ and Wicki, J and RUPITZ, K and Withers, SG}
}
