beta-D-xylosidase from Bacillus pumilus PRL B12: hydrolysis of aryl beta-D-xylopyranosides.

The influence of substituents on the binding and hydrolysis of several substituted beta-D-xylopyranosides by beta-D-xylosidase from Bacillus pumilus PRL B12 has been investigated. From a comparison of the inhibition constants of 1-thio-beta-D-xylopyranosides with the apparent Michaelis-Menten constants of the substrates, it followed that the latter constants are good approximations of the true equilibrium constants. The influence of the substituent on the rate and activation parameters is small. The results are in agreement with, but do not prove, a one-step mechanism without the formation of a glycosyl-enzyme intermediate.