@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} }