| A_amylase_inhib | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor hoe-467a | |||||||||
| Identifiers | |||||||||
| Symbol | A_amylase_inhib | ||||||||
| Pfam | PF01356 | ||||||||
| InterPro | IPR000833 | ||||||||
| SCOP2 | 1hoe / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, alpha-amylase inhibitor (or α-...) 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.
They are found in raw plants/herbs such as cinnamon and bacteria (containing the inhibitor acarbose).[1][2]
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.[citation needed]
- ^ Moreira, Fernanda Duarte; Reis, Caio Eduardo Gonçalves; Gallassi, Andrea Donatti; Moreira, Daniel Carneiro; Welker, Alexis Fonseca (2024-10-09). Dardari, Dured (ed.). "Suppression of the postprandial hyperglycemia in patients with type 2 diabetes by a raw medicinal herb powder is weakened when consumed in ordinary hard gelatin capsules: A randomized crossover clinical trial". PLOS ONE. 19 (10): e0311501. doi:10.1371/journal.pone.0311501. ISSN 1932-6203. PMC 11463819. PMID 39383145.
- ^ Hayward, Nicholas J.; McDougall, Gordon J.; Farag, Sara; Allwood, J. William; Austin, Ceri; Campbell, Fiona; Horgan, Graham; Ranawana, Viren (December 2019). "Cinnamon Shows Antidiabetic Properties that Are Species-Specific: Effects on Enzyme Activity Inhibition and Starch Digestion". Plant Foods for Human Nutrition. 74 (4): 544–552. doi:10.1007/s11130-019-00760-8. ISSN 0921-9668. PMC 6900266. PMID 31372918.
- ^ König V, Vértesy L, Schneider TR (October 2003). "Structure of the alpha-amylase inhibitor tendamistat at 0.93 A". Acta Crystallogr. D. 59 (Pt 10): 1737–43. doi:10.1107/S0907444903015828. PMID 14501112.