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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
2008
关键词crystal structure acetyltransferase substrate binding UDP-N-acetylglucosamine SEROTONIN N-ACETYLTRANSFERASE CATALYTIC MECHANISM COENZYME-A COMPLEX SUPERFAMILY GCN5
DOI10.1016/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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