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| Title | Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition. |
|---|---|
| Journal, issue, pages | J Enzyme Inhib Med Chem, Vol. 41, Issue 1, Page 2612391, Year 2026 |
| Publish date | Jan 14, 2026 |
Authors | Ken Watanabe / Takayoshi Tagami / Chihiro Biwa / Masato Kawasaki / Naruhiko Adachi / Toshio Moriya / Toshiya Senda / Masayuki Okuyama / ![]() |
| PubMed Abstract | 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. |
External links | J Enzyme Inhib Med Chem / PubMed:41534875 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.77 - 3.17 Å |
| Structure data | EMDB-62652, PDB-9kz6: EMDB-62653, PDB-9kz7: |
| Chemicals | ![]() ChemComp-NAG: |
| Source |
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Keywords | HYDROLASE / alpha-glucosidase |
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