Slow-Binding Inhibition of Branching Enzyme by the Pseudooligosaccharide BAY e4609

Branching enzyme from Escherichia coli is shown to be inhibited by the pseudooligosaccharide BAY e4609. The mechanism of binding is studied in detail by kinetics using reduced amylose as substrate. Lineweaver–Burk plots suggest the mechanism of a noncompetitive or slow-binding inhibitor. Further stu...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2000-02, Vol.374 (1), p.73-78
Main Authors: Binderup, Kim, Libessart, Nathalie, Preiss, Jack
Format: Article
Language:English
Subjects:
1,4-alpha-Glucan Branching Enzyme - analysis
1,4-alpha-Glucan Branching Enzyme - antagonists & inhibitors
1,4-alpha-Glucan Branching Enzyme - metabolism
acarbose
amylolytic family
Amylose - metabolism
BAY e4609
branching enzyme
Chromatography, Gel
Escherichia coli - enzymology
Glycogen - metabolism
Kinetics
Oligo-1,6-Glucosidase - analysis
Oligo-1,6-Glucosidase - antagonists & inhibitors
Oligo-1,6-Glucosidase - metabolism
Oligosaccharides - metabolism
Oligosaccharides - pharmacology
Protein Binding - drug effects
slow-binding inhibition
Substrate Specificity
Temperature
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Summary:Branching enzyme from Escherichia coli is shown to be inhibited by the pseudooligosaccharide BAY e4609. The mechanism of binding is studied in detail by kinetics using reduced amylose as substrate. Lineweaver–Burk plots suggest the mechanism of a noncompetitive or slow-binding inhibitor. Further studies by progress curves and rate of loss of branching activity allows us to conclude BAY e4609 as being a slow-binding inhibitor of branching enzyme. We discuss how these results parallel the inhibition of α-amylase by acarbose and the significance of branching enzyme as belonging to the amylolytic family.
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1999.1580