| 词条 | Alpha amylase inhibitor |
| 释义 |
| Symbol = A_amylase_inhib | Name = A_amylase_inhib | image = PDB 1hoe EBI.jpg | width = | caption = crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a | Pfam = PF01356 | Pfam_clan = | InterPro = IPR000833 | SMART = | PROSITE = | MEROPS = | SCOP = 1hoe | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, alpha-amylase inhibitor is a protein family which inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. This family of inhibitors 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.[1] 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. References1. ^{{cite journal |vauthors=König V, Vértesy L, Schneider TR | title = Structure of the alpha-amylase inhibitor tendamistat at 0.93 A | journal = Acta Crystallogr. D | volume = 59 | issue = Pt 10 | pages = 1737–43 |date=October 2003 | pmid = 14501112 | doi = 10.1107/S0907444903015828| url = }} {{InterPro content|IPR000833}} 1 : Protein domains |
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