Inhibition of porcine small intestinal sucrase by valienamine

J Enzyme Inhib Med Chem. 2005 Feb;20(1):49-53. doi: 10.1080/14756360400015264.

Abstract

Valienamine, an aminocyclitol, has been isolated from the enzymolysis broth of validamycins. The absolute configuration of valienamine is similar to that of alpha-D-glucose. The inhibitory effect of this amino-sugar analog of alpha-D-glucose, valienamine, on porcine small intestinal sucrase was examined. Valienamine was found to be potent, competitive reversible inhibitor of porcine small intestinal sucrase in vitro with an IC50 value of 1.17 x 10(-3)M. Valienamine also exhibited dose-dependent, instantaneous inhibition of porcine small intestinal sucrase. The inhibition of porcine small intestinal sucrase by valienamine was pH-independent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cyclohexenes
  • Hexosamines / isolation & purification
  • Hexosamines / pharmacology*
  • Hydrogen-Ion Concentration
  • Inositol / analogs & derivatives
  • Inositol / chemistry
  • Inositol / metabolism*
  • Intestine, Small / drug effects*
  • Intestine, Small / enzymology*
  • Sucrase / antagonists & inhibitors*
  • Swine

Substances

  • Cyclohexenes
  • Hexosamines
  • valienamine
  • Inositol
  • validamycins
  • Sucrase