Sandbox Ruth01
From Proteopedia
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"Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases. | "Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. 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 <ref> pmid 14501112</ref> <scene name='Sandbox_Ruth01/Tandemistat_no_changes/1'> | + | 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 <ref> pmid 14501112</ref> <scene name='Sandbox_Ruth01/Tandemistat_no_changes/1'>Tendamistat</scene>. 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." |
Revision as of 11:02, 6 September 2012
Your Heading Here (maybe something like 'Structure')
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