The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Structural insight into substrate specificity of human intestinal maltase-glucoamylase
Open accessAbstract
Human maltase-glucoamylase (MGAM) hydrolyzes linear alpha-1,4-linked oligosaccharide substrates, playing a crucial role in the production of glucose in the human lumen and acting as an efficient drug target for type 2 diabetes and obesity. The amino- and carboxyl-terminal portions of MGAM (MGAM-N and MGAM-C) carry out the same catalytic reaction but have different substrate specificities. In this study, we report crystal structures of MGAM-C alone at a resolution of 3.1 Å, and in complex with its inhibitor acarbose at a resolution of 2.9 Å. Structural studies, combined with biochemical analysis, revealed that a segment of 21 amino acids in the active site of MGAM-C forms additional sugar subsites (+ 2 and + 3 subsites), accounting for the preference for longer substrates of MAGM-C compared with that of MGAM-N. Moreover, we discovered that a single mutation of Trp1251 to tyrosine in MGAM-C imparts a novel catalytic ability to digest branched alpha-1,6-linked oligosaccharides. These results provide important information for understanding the substrate specificity of alpha-glucosidases during the process of terminal starch digestion, and for designing more efficient drugs to control type 2 diabetes or obesity.
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Metadata
- Authors
- Ren, L., Qin, X., Cao, X., Wang, L., Bai, F., Bai, G., & Shen, Y.
- Venue
- Protein & Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-10
- Volume
- 2
- Issue
- 10
- Pages
- 827-836
- ISSN
- 1674-800X (ISSN-L)
- 1674-8018
- OpenAlex
- W1969058624
- Cited by
- 253
- References
- 26
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ren, L., Qin, X., Cao, X., Wang, L., Bai, F., Bai, G., & Shen, Y. (2011). Structural insight into substrate specificity of human intestinal maltase-glucoamylase. Protein & Cell. https://doi.org/10.1007/s13238-011-1105-3
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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