5TMA

Zymomonas mobilis pyruvate decarboxylase mutant PDC-2.3

5TMA の概要

• エントリーDOI: 10.2210/pdb5tma/pdb
• 分子名称: Pyruvate decarboxylase, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: pyruvate decarboxylase, pdc, mutant, engineered, thermostable, cell adhesion
• 由来する生物種: Zymomonas mobilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 128430.74

構造登録者

Alahuhta, P.M.,Lunin, V.V. (登録日: 2016-10-12, 公開日: 2017-10-18, 最終更新日: 2023-10-04)

主引用文献

Sammond, D.W.,Kastelowitz, N.,Donohoe, B.S.,Alahuhta, M.,Lunin, V.V.,Chung, D.,Sarai, N.S.,Yin, H.,Mittal, A.,Himmel, M.E.,Guss, A.M.,Bomble, Y.J.
An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme.
Biotechnol Biofuels, 11:189-189, 2018

PubMed Abstract: Strategies for maximizing the microbial production of bio-based chemicals and fuels include eliminating branched points to streamline metabolic pathways. While this is often achieved by removing key enzymes, the introduction of nonnative enzymes can provide metabolic shortcuts, bypassing branched points to decrease the production of undesired side-products. Pyruvate decarboxylase (PDC) can provide such a shortcut in industrially promising thermophilic organisms; yet to date, this enzyme has not been found in any thermophilic organism. Incorporating nonnative enzymes into host organisms can be challenging in cases such as this, where the enzyme has evolved in a very different environment from that of the host.

PubMed: 30002729
DOI: 10.1186/s13068-018-1178-9

実験手法

X-RAY DIFFRACTION (1.67 Å)