Tendemistat description based on scoop, koning et al. (2003)[1] and Vertesy et al. (1984)[2] :
Tendemistat is produced by alpha-amylase inhibitor which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex. The inhibitor has no action on plant and microbial alpha amylases.
A crystal structure has been determined for tendamistat the 74-amino acid inhibitor produced by Streptomyces tendae that targets a wide range of mammalian alpha-amylases [3] . The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity."
A crystal structure of tendemistat (green) with a pig pancreatic alpha-amylase (orange) is also available [4] .
Tendamistat belongs to the scoop class of all beta proteins since it is exclusivly formed of beta sheets (light blue) .
