6YAJ

Split gene transketolase, inactive beta4 tetramer

これはPDB形式変換不可エントリーです。

6YAJ の概要

• エントリーDOI: 10.2210/pdb6yaj/pdb
• 分子名称: C-terminal chain of split transketolase from Carboxydothermus hydrogenoformans, 1,2-ETHANEDIOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: hyperthermophilic, split-gene transketolase, thermal stability, industrial applications, transferase
• 由来する生物種: Carboxydothermus hydrogenoformans
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145643.06

構造登録者

Isupov, M.N.,Littlechild, J.A.,James, P. (登録日: 2020-03-12, 公開日: 2020-11-25, 最終更新日: 2024-01-24)

主引用文献

James, P.,Isupov, M.N.,De Rose, S.A.,Sayer, C.,Cole, I.S.,Littlechild, J.A.
A 'Split-Gene' Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans : Structure and Biochemical Characterization.
Front Microbiol, 11:592353-592353, 2020

PubMed Abstract: A novel transketolase has been reconstituted from two separate polypeptide chains encoded by a 'split-gene' identified in the genome of the hyperthermophilic bacterium, . The reconstituted active αβ tetrameric enzyme has been biochemically characterized and its activity has been determined using a range of aldehydes including glycolaldehyde, phenylacetaldehyde and cyclohexanecarboxaldehyde as the ketol acceptor and hydroxypyruvate as the donor. This reaction proceeds to near 100% completion due to the release of the product carbon dioxide and can be used for the synthesis of a range of sugars of interest to the pharmaceutical industry. This novel reconstituted transketolase is thermally stable with no loss of activity after incubation for 1 h at 70°C and is stable after 1 h incubation with 50% of the organic solvents methanol, ethanol, isopropanol, DMSO, acetonitrile and acetone. The X-ray structure of the holo reconstituted αβ tetrameric transketolase has been determined to 1.4 Å resolution. In addition, the structure of an inactive tetrameric β protein has been determined to 1.9 Å resolution. The structure of the active reconstituted αβ enzyme has been compared to the structures of related enzymes; the E1 component of the pyruvate dehydrogenase complex and D-xylulose-5-phosphate synthase, in an attempt to rationalize differences in structure and substrate specificity between these enzymes. This is the first example of a reconstituted 'split-gene' transketolase to be biochemically and structurally characterized allowing its potential for industrial biocatalysis to be evaluated.

PubMed: 33193259
DOI: 10.3389/fmicb.2020.592353

実験手法

X-RAY DIFFRACTION (1.9 Å)