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 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 alpha-amylase by acarbose and the significance of branching enzyme as belonging to the amylolytic family.
Binderup
K
K
Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824, USA.
Libessart
N
N
Preiss
J
J
D015061:1,4-alpha-Glucan Branching Enzyme / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism; D000688:Amylose / Q000378:metabolism; D002850:Chromatography, Gel; D004926:Escherichia coli / Q000201:enzymology; D006003:Glycogen / Q000378:metabolism; D007700:Kinetics; D009834:Oligo-1,6-Glucosidase / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D013379:Substrate Specificity; D013696:Temperature
D009844:Oligosaccharides; C030114:Aplanin; D006003:Glycogen; D000688:Amylose; D015061:1,4-alpha-Glucan Branching Enzyme; D009834:Oligo-1,6-Glucosidase