The following Tendemistat description is based on scoop, koning et al. (2003)[1] and Vertesy et al. (1984)[2] :
Tendemistat is a 74 amino acid protein produced by Streptomyces tendae. Though it has been suggested to perform a regulatory role in its natural producer[3], its native purpose remains unclear. However, tendamistat was found to be a potentalpha-amylase inhibitor which specifically affects mammalian enzymes, and has no effect on alpha-amylases from other sources (e.g. plant and bacteria). Tendamistat (green) forms a tight stoichiometric 1:1 complex with alpha amylase (orange), a crystal structure of the complex was determined to a 2.5 A resolution [4] .
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 [5] . 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 [6] .
Tendamistat belongs to the scoop class of all beta proteins since it is exclusivly formed of beta sheets (light blue) .
