Hydrolysis of para-substituted phenyl-.BETA.-D-xylosides by .BETA.-xylosidase from Malbranchea pulchella var. sulfurea No. 48.
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چکیده
منابع مشابه
Stimulation of synthesis of free chondroitin sulfate chains by beta-D-xylosides in cultured cells.
Beta-Xylosides stimulate 2- to 6-fold the synthesis of glycosaminoglycans by three types of nonconnective tissue cells (RG-C6, NB41A, and rat hepatoma cells, and normal and simian virus 40 (SV40)-transformed normal human skin fibroblasts. The effect, which is specific for the anomeric linkage and the glycone, is observed in the presence and absence of puromycin. Beta-Xylosides may substitute f...
متن کاملBiochemical properties of a beta-xylosidase from Clostridium cellulolyticum.
A 43-kDa beta-xylosidase from Clostridium cellulolyticum was purified to homogeneity. The enzyme releases xylose from p-nitrophenylxylose and xylodextrins with a degree of polymerization ranging between 2 and 5. The N-terminal amino acid sequence of the enzyme showed homologies with three other bacterial beta-xylosidases. By proton nuclear magnetic resonance spectroscopy, the enzyme was found t...
متن کاملBeta-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43.
Beta-D-xylosidase from the ruminal anaerobic bacterium, Selenomonas ruminantium (SXA), catalyzes hydrolysis of beta-1,4-xylooligosacharides and has potential utility in saccharification processes. The enzyme, heterologously produced in Escherichia coli and purified to homogeneity, has an isoelectric point of approx 4.4, an intact N terminus, and a Stokes radius that defines a homotetramer. SXA ...
متن کاملAminoalcohols as probes of the two-subsite active site of beta-D-xylosidase from Selenomonas ruminantium.
Catalysis and inhibitor binding by the GH43 beta-xylosidase are governed by the protonation states of catalytic base (D14, pK(a) 5.0) and catalytic acid (E186, pK(a) 7.2) which reside in subsite -1 of the two-subsite active site. Cationic aminoalcohols are shown to bind exclusively to subsite -1 of the catalytically-inactive, dianionic enzyme (D14(-)E186(-)). Enzyme (E) and aminoalcohols (A) fo...
متن کاملBeta-D-xylosidase from Selenomonas ruminantium: catalyzed reactions with natural and artificial substrates.
Catalytically efficient beta-D-xylosidase from Selenomonas ruminantium (SXA) exhibits pK (a)s 5 and 7 (assigned to catalytic base, D14, and catalytic acid, E186) for k (cat)/K (m) with substrates 1,4-beta-D-xylobiose (X2) and 1,4-beta-D-xylotriose (X3). Catalytically inactive, dianionic SXA (D14(-)E186(-)) has threefold lower affinity than catalytically active, monoanionic SXA (D14(-)E186(H)) f...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1981
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.45.1603