Ontology highlight
ABSTRACT:
SUBMITTER: Ren L
PROVIDER: S-EPMC4875297 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
Ren Limei L Qin Xiaohong X Cao Xiaofang X Wang Lele L Bai Fang F Bai Gang G Shen Yuequan Y
Protein & cell 20111001 10
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 it ...[more]