Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/86611
標題: Insights into the binding specificity and catalytic mechanism ofN-acetylhexosamine 1-phosphate kinases through multiple reaction complexes
作者: Wang, Kuei-Chen
Lyu, Syue-Yi
Liu, Yu-Chen
Chang, Chin-Yuan
Wu, Chang-Jer
Li, Tsung-Lin
關鍵字: N-acetylhexosamine 1-phosphate kinase
bifidobacteria
multiple reaction complexes
Acetylglucosamine
Adenosine Diphosphate
Adenosine Triphosphate
Bifidobacterium
Binding Sites
Crystallography, X-Ray
Magnesium
Models, Molecular
Mutagenesis, Site-Directed
Phosphotransferases
Protein Conformation
Substrate Specificity
摘要: Utilization of N-acetylhexosamine in bifidobacteria requires the specific lacto-N-biose/galacto-N-biose pathway, a pathway differing from the Leloir pathway while establishing symbiosis between humans and bifidobacteria. The gene lnpB in the pathway encodes a novel hexosamine kinase NahK, which catalyzes the formation of N-acetylhexosamine 1-phosphate (GlcNAc-1P/GalNAc-1P). In this report, seven three-dimensional structures of NahK in complex with GlcNAc, GalNAc, GlcNAc-1P, GlcNAc/AMPPNP and GlcNAc-1P/ADP from both Bifidobacterium longum (JCM1217) and B. infantis (ATCC15697) were solved at resolutions of 1.5-2.2 Å. NahK is a monomer in solution, and its polypeptide folds in a crescent-like architecture subdivided into two domains by a deep cleft. The NahK structures presented here represent the first multiple reaction complexes of the enzyme. This structural information reveals the molecular basis for the recognition of the given substrates and products, GlcNAc/GalNAc, GlcNAc-1P/GalNAc-1P, ATP/ADP and Mg(2+), and provides insights into the catalytic mechanism, enabling NahK and mutants thereof to form a choice of biocatalysts for enzymatic and chemoenzymatic synthesis of carbohydrates.
URI: http://hdl.handle.net/11455/86611
ISSN: 1399-0047
1399-0047
Appears in Collections:生物科技發展中心

文件中的檔案:

取得全文請前往華藝線上圖書館



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.