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

作者信息

Kersters-Hilderson H, Van Doorslaer E, De Bruyne C K

出版信息

Carbohydr Res. 1978 Sep;65(2):219-27. doi: 10.1016/s0008-6215(00)84313-x.

DOI:10.1016/s0008-6215(00)84313-x
PMID:698980
Abstract

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.

摘要

相似文献

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beta-D-xylosidase from Bacillus pumilus PRL B12: hydrolysis of aryl beta-D-xylopyranosides.
Carbohydr Res. 1978 Sep;65(2):219-27. doi: 10.1016/s0008-6215(00)84313-x.
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Binding of n-alkyl beta-D-xylopyranosides and n-alkyl 1-thio-beta-D-xylopyranosides to beta-D-xylosidase from Bacillus pumilus PRL B12.
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Hydrolysis of para-substituted aryl beta-D-xylopyranosides and beta(1 leads to 4)xylo-oligosaccharides by an induced beta-D-xylosidase from Bacillus pumilus PRL B12 [proceedings].
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Transfer reactions catalyzed by beta-D-xylosidase from Penicillium wortmanni.由特异青霉β-D-木糖苷酶催化的转移反应。
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