Inhibition of β-galactosidases with mono- and disaccharides

It was demonstrated that, in reactions of the hydrolysis of model substrate 2-nitrophenyl-β-D-galactopyranoside (2-NPGP) monosaccharides D-fructose and D-xylose with hydroxyl substituents oppositely directed at the neighboring carbon atoms in the furan ring, as in D-glucose, act as noncompetitive in...

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Bibliographic Details
Published in:Russian Journal of Physical Chemistry A 2010, Vol.84 (1), p.118-122
Main Authors: Pilipenko, O. S., Atyaksheva, L. F., Chukhrai, E. S.
Format: Article
Language:English
Subjects:
Biophysical Chemistry
Chemistry
Chemistry and Materials Science
Physical Chemistry
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Summary:It was demonstrated that, in reactions of the hydrolysis of model substrate 2-nitrophenyl-β-D-galactopyranoside (2-NPGP) monosaccharides D-fructose and D-xylose with hydroxyl substituents oppositely directed at the neighboring carbon atoms in the furan ring, as in D-glucose, act as noncompetitive inhibitors of β-galactosidase from E. coli ; for mushroom, β-galactosidases from P. canescens and A. oryzae D-galactose is a stronger inhibitor. It was also found that the inhibition constant is the highest in the case of the most active enzyme ( E. coli ) and is the lowest for the least active one ( P. canescens ).
ISSN:0036-0244
1531-863X
DOI:10.1134/S003602441001022X