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-Structure paper
| タイトル | Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition. |
|---|---|
| ジャーナル・号・ページ | J Enzyme Inhib Med Chem, Vol. 41, Issue 1, Page 2612391, Year 2026 |
| 掲載日 | 2026年1月14日 |
著者 | Ken Watanabe / Takayoshi Tagami / Chihiro Biwa / Masato Kawasaki / Naruhiko Adachi / Toshio Moriya / Toshiya Senda / Masayuki Okuyama / ![]() |
| PubMed 要旨 | Maltase-glucoamylase (MGAM) is a small-intestinal enzyme comprising two tandem α-glucosidase units, NtMGAM and CtMGAM, each capable of hydrolysing maltodextrins into glucose. MGAM serves as a ...Maltase-glucoamylase (MGAM) is a small-intestinal enzyme comprising two tandem α-glucosidase units, NtMGAM and CtMGAM, each capable of hydrolysing maltodextrins into glucose. MGAM serves as a therapeutic target for managing postprandial hyperglycaemia; comprehensive insights into its full-length three-dimensional structure and inhibitor kinetics remains limited. Here, we demonstrate that the α-glucosidase in porcine serum is comparable to that encoded by the MGAM gene. Using cryo-electron microscopy, we determined the complex structure of serum MGAM with the inhibitor acarviosyl-maltotriose (AC5), which was found to bind exclusively to the active sites of each unit, confirming the presence of independent catalytic sites. AC5 was shown to exhibit mixed-type inhibition towards full-length serum MGAM and competitive inhibition against both recombinant NtMGAM and CtMGAM. The apparent mixed-type inhibition can be more accurately attributed to dual competitive inhibition mechanisms. These findings contribute to the advancement of functional foods and therapeutic interventions for postprandial hyperglycaemia and type 2 diabetes. |
リンク | J Enzyme Inhib Med Chem / PubMed:41534875 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.77 - 3.17 Å |
| 構造データ | EMDB-62652, PDB-9kz6: EMDB-62653, PDB-9kz7: |
| 化合物 | ![]() ChemComp-NAG: |
| 由来 |
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キーワード | HYDROLASE / alpha-glucosidase |
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