---
pmid: '19059404'
title: Structural analysis of human glutamine:fructose-6-phosphate amidotransferase,
  a key regulator in type 2 diabetes.
authors:
- Nakaishi Y
- Bando M
- Shimizu H
- Watanabe K
- Goto F
- Tsuge H
- Kondo K
- Komatsu M
journal: FEBS Lett
year: '2009'
full_text_available: false
doi: 10.1016/j.febslet.2008.11.041
pubmed_publication_types:
- Journal Article
publication_type: PRIMARY_RESEARCH
---

# Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes.
**Authors:** Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M
**Journal:** FEBS Lett (2009)
**DOI:** [10.1016/j.febslet.2008.11.041](https://doi.org/10.1016/j.febslet.2008.11.041)

## Abstract

1. FEBS Lett. 2009 Jan 5;583(1):163-7. doi: 10.1016/j.febslet.2008.11.041. Epub
2008 Dec 6.

Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a
key regulator in type 2 diabetes.

Nakaishi Y(1), Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu
M.

Author information:
(1)Medicinal Chemistry Research Institute, Otsuka Pharmaceutical Co. Ltd.,
Kawauchi-cho, Tokushima, Japan. y_nakaishi@research.otsuka.co.jp

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.

DOI: 10.1016/j.febslet.2008.11.041
PMID: 19059404 [Indexed for MEDLINE]