7X78

L-fuculose 1-phosphate aldolase

7X78 の概要

• エントリーDOI: 10.2210/pdb7x78/pdb
• 分子名称: L-fuculose phosphate aldolase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: fuculose 1-phosphate aldolase, enzyme activity, klebsiella pneumoniae., lyase
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24079.75

構造登録者

Lou, X.,Zhang, Q.,Bartlam, M. (登録日: 2022-03-09, 公開日: 2022-04-13, 最終更新日: 2023-11-29)

主引用文献

Lou, X.,Zhang, J.,Liu, S.,Wang, R.,Li, W.,Liu, R.,Zhang, Q.,Bartlam, M.
Structural characterization of an L-fuculose-1-phosphate aldolase from Klebsiella pneumoniae.
Biochem.Biophys.Res.Commun., 607:15-19, 2022

PubMed Abstract: Fuculose phosphate aldolases play an important role in glycolysis and gluconeogenesis pathways. L-fuculose 1-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate to DHAP and L-lactaldehyde. Class II aldolases found in bacteria are linked to pathogenesis of human pathogens, and have potential applications in the biosynthesis of carbohydrates and other chiral compounds. Here we report the structure of a putative L-fuculose 1-phosphate aldolase (KpFucA) from the nosocomial pathogen Klebsiella pneumoniae to 1.85 Å resolution. The enzyme crystallizes in space group P422 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis confirms that KpFucA is a tetramer in solution. A magnesium ion cofactor and sulfate ion were identified in the active pocket. Enzyme activity assays confirmed that KpFcuA has a strong preference for L-fuculose 1-phosphate as a substrate, but can also catalyze the cleavage of fructose-1,6-bisphosphate and glucose-6-phosphate. This work should provide a starting point for further investigation of the role of KpFucA in K. pneumoniae pathogenesis or in industrial applications.

PubMed: 35366538
DOI: 10.1016/j.bbrc.2022.03.127

実験手法

X-RAY DIFFRACTION (1.85 Å)