The inhibition of human salivary alpha-amylase by type II alpha-amylase inhibitor from Triticum aestivum is competitive, slow and tight-binding.
A kinetic analysis of the inhibition of human salivary alpha-amylase (EC 3.2.1.1) by wheat seed (Triticum aestivum) type II alpha-amylase inhibitor revealed the inhibition was slow and tight-binding. The inhibition was competitive with an inhibition binding constant of the alpha-amylase inhibitor for alpha-amylase of 0.29 nM. The KM of alpha-amylase for soluble starch (calculated per mole of alpha-1,4 linked maltose residues) was 5.87 mM.
Goff
D J
DJ
Department of Chemistry, Dartmouth College Hanover, New Hampshire 03755, USA.
Kull
F J
FJ
D001667:Binding, Competitive; D004791:Enzyme Inhibitors / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D007700:Kinetics; D010940:Plant Proteins / Q000378:metabolism / Q000494:pharmacology*; D012469:Salivary Glands / Q000201:enzymology*; D012639:Seeds / Q000737:chemistry; D014908:Triticum / Q000737:chemistry; D000516:alpha-Amylases / Q000037:antagonists & inhibitors* / Q000378:metabolism
D004791:Enzyme Inhibitors; D010940:Plant Proteins; D000516:alpha-Amylases