4TSK

Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius

4TSK の概要

• エントリーDOI: 10.2210/pdb4tsk/pdb
• 分子名称: Ketol-acid reductoisomerase, MAGNESIUM ION, L(+)-TARTARIC ACID, ... (5 entities in total)
• 機能のキーワード: ketol-acid reductoisomerase, rossmann fold, nadph-binding, oxidoreductase, isomerase
• 由来する生物種: Alicyclobacillus acidocaldarius subsp. acidocaldarius
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39753.53

構造登録者

Cahn, J.K.B.,Brinkmann-Chen, S.,Arnold, F.H. (登録日: 2014-06-18, 公開日: 2014-07-09, 最終更新日: 2023-09-27)

主引用文献

Brinkmann-Chen, S.,Cahn, J.K.,Arnold, F.H.
Uncovering rare NADH-preferring ketol-acid reductoisomerases.
Metab. Eng., 26C:17-22, 2014

PubMed Abstract: All members of the ketol-acid reductoisomerase (KARI) enzyme family characterized to date have been shown to prefer the nicotinamide adenine dinucleotide phosphate hydride (NADPH) cofactor to nicotinamide adenine dinucleotide hydride (NADH). However, KARIs with the reversed cofactor preference are desirable for industrial applications, including anaerobic fermentation to produce branched-chain amino acids. By applying insights gained from structural and engineering studies of this enzyme family to a comprehensive multiple sequence alignment of KARIs, we identified putative NADH-utilizing KARIs and characterized eight whose catalytic efficiencies using NADH were equal to or greater than NADPH. These are the first naturally NADH-preferring KARIs reported and demonstrate that this property has evolved independently multiple times, using strategies unlike those used previously in the laboratory to engineer a KARI cofactor switch.

PubMed: 25172159
DOI: 10.1016/j.ymben.2014.08.003

実験手法

X-RAY DIFFRACTION (2.5 Å)