We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
- Authors
Wang, Juan; Liu, Xiang; Liang, Yu-He; Li, Lan-Fen; Su, Xiao-Dong
- Abstract
Abstract: Glucosamine-6-phosphate (GlcN6P) N-acetyltransferase 1 (GNA1) is a key enzyme in the pathway toward biosynthesis of UDP-N-acetylglucosamine, an important donor substrate for N-linked glycosylation. GNA1 catalyzes the formation of N-acetylglucosamine-6-phosphate (GlcNAc6P) from acetyl-CoA (AcCoA) and the acceptor substrate GlcN6P. Here, we report crystal structures of human GNA1, including apo GNA1, the GNA1-GlcN6P complex and an E156A mutant. Our work showed that GlcN6P binds to GNA1 without the help of AcCoA binding. Structural analyses and mutagenesis studies have shed lights on the charge distribution in the GlcN6P binding pocket, and an important role for Glu156 in the substrate binding. Hence, these findings have broadened our knowledge of structural features required for the substrate affinity of GNA1. Structured summary: MINT:6700314: GNA1 (uniprotkb:Q96EK6) and GNA1 (uniprotkb:Q96EK6) bind (MI:0407) by X-ray crystallography (MI:0114)
- Subjects
ENZYMES; BIOSYNTHESIS; SUBSTRATES (Materials science); STRUCTURAL analysis (Science); MUTAGENESIS; X-ray crystallography
- Publication
FEBS Letters, 2008, Vol 582, Issue 20, p2973
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2008.07.040