Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1 | |
Wang, Juan ; Liu, Xiang ; Liang, Yu-He ; Li, Lan-Fen ; Su, Xiao-Dong | |
刊名 | 欧洲生化学会联合会快报
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2008 | |
关键词 | crystal structure acetyltransferase substrate binding UDP-N-acetylglucosamine SEROTONIN N-ACETYLTRANSFERASE CATALYTIC MECHANISM COENZYME-A COMPLEX SUPERFAMILY GCN5 |
DOI | 10.1016/j.febslet.2008.07.040 |
英文摘要 | 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.; Biochemistry & Molecular Biology; Biophysics; Cell Biology; SCI(E); PubMed; 5; ARTICLE; 20; 2973-2978; 582 |
语种 | 英语 |
内容类型 | 期刊论文 |
源URL | [http://ir.pku.edu.cn/handle/20.500.11897/162594] ![]() |
专题 | 生命科学学院 |
推荐引用方式 GB/T 7714 | Wang, Juan,Liu, Xiang,Liang, Yu-He,et al. Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1[J]. 欧洲生化学会联合会快报,2008. |
APA | Wang, Juan,Liu, Xiang,Liang, Yu-He,Li, Lan-Fen,&Su, Xiao-Dong.(2008).Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1.欧洲生化学会联合会快报. |
MLA | Wang, Juan,et al."Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1".欧洲生化学会联合会快报 (2008). |
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