beta-D-xylosidase from Penicillium wortmanni: binding and hydrolysis of alkyl and aryl 1-oxygen and 1-thio-beta-D-xylopyranosides.
The influence of the chain length in n-alkyl beta-D-xylopyranosides and of the para substituents in aryl beta-D-xylopyranosides on the kinetic parameters (Ka, V) for hydrolysis of these substrates by a beta-D-xylosidase from Penicillium wortmanni, has been investigated. Binding of the corresponding 1-thio derivatives as competitive inhibitors (Ki) was studied for comparative purposes. For the n-alkyl substrates, a slight dependency of V on the chain length is noted, whereas the aryl beta-D-xylopyranosides show nearly constant V values. The influence of the aglycon on Ka and Ki values is complex; for the n-alkyl derivatives the contribution of the hydrophobicity of the aliphatic chain seems predominant, although steric factors cannot be neglected. These results, together with previous observations, can tentatively be interpreted in terms of a double-displacement mechanism.
D000495:Allosteric Site; D001665:Binding Sites; D001667:Binding, Competitive; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D010407:Penicillium / Q000201:enzymology*; D013379:Substrate Specificity; D013865:Thioglycosides; D014995:Xylosidases / Q000378:metabolism*
D013865:Thioglycosides; D006026:Glycoside Hydrolases; D014995:Xylosidases