Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872012 | FEBS Letters | 2009 | 5 Pages |
Abstract
Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Yuichiro Nakaishi, Masahiko Bando, Hiroshi Shimizu, Kenji Watanabe, Fumitaka Goto, Hideaki Tsuge, Kazumi Kondo, Makoto Komatsu,