7NZP

D-lyxose isomerase from the hyperthermophilic archaeon Thermofilum sp complexed with D-fructose

これはPDB形式変換不可エントリーです。

7NZP の概要

• エントリーDOI: 10.2210/pdb7nzp/pdb
• 分子名称: D-lyxose/D-mannose family sugar isomerase, beta-D-fructofuranose, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: complex, thermostability, biocatalysis, isomerase
• 由来する生物種: Thermofilum sp. ex4484_79
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48452.82

構造登録者

De Rose, S.A.,Isupov, M.N.,Littlechild, J.A.,Schoenheit, P. (登録日: 2021-03-24, 公開日: 2021-10-13, 最終更新日: 2024-11-06)

主引用文献

De Rose, S.A.,Kuprat, T.,Isupov, M.N.,Reinhardt, A.,Schonheit, P.,Littlechild, J.A.
Biochemical and Structural Characterisation of a Novel D-Lyxose Isomerase From the Hyperthermophilic Archaeon Thermofilum sp.
Front Bioeng Biotechnol, 9:711487-711487, 2021

PubMed Abstract: A novel D-lyxose isomerase has been identified within the genome of a hyperthermophilic archaeon belonging to the species. The enzyme has been cloned and over-expressed in and biochemically characterised. This enzyme differs from other enzymes of this class in that it is highly specific for the substrate D-lyxose, showing less than 2% activity towards mannose and other substrates reported for lyxose isomerases. This is the most thermoactive and thermostable lyxose isomerase reported to date, showing activity above 95°C and retaining 60% of its activity after 60 min incubation at 80°C. This lyxose isomerase is stable in the presence of 50% (v/v) of solvents ethanol, methanol, acetonitrile and DMSO. The crystal structure of the enzyme has been resolved to 1.4-1.7 A. resolution in the ligand-free form and in complexes with both of the slowly reacting sugar substrates mannose and fructose. This thermophilic lyxose isomerase is stabilised by a disulfide bond between the two monomers of the dimeric enzyme and increased hydrophobicity at the dimer interface. These overall properties of high substrate specificity, thermostability and solvent tolerance make this lyxose isomerase enzyme a good candidate for potential industrial applications.

PubMed: 34422783
DOI: 10.3389/fbioe.2021.711487

実験手法

X-RAY DIFFRACTION (1.345 Å)