6CSJ

Structure of a Bacillus coagulans polyol dehydrogenase double mutant with an acquired D-lactate dehydrogenase activity

6CSJ の概要

• エントリーDOI: 10.2210/pdb6csj/pdb
• 分子名称: Glycerol dehydrogenase (2 entities in total)
• 機能のキーワード: polyol dehydrogenase, oxidoreductase
• 由来する生物種: Bacillus coagulans
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 314895.78

構造登録者

Hurlbert, J.C.,St.John, F.J. (登録日: 2018-03-20, 公開日: 2019-07-03, 最終更新日: 2023-10-04)

主引用文献

Chauliac, D.,Wang, Q.,St John, F.J.,Jones, G.,Hurlbert, J.C.,Ingram, L.O.,Shanmugam, K.T.
Kinetic characterization and structure analysis of an altered polyol dehydrogenase with d-lactate dehydrogenase activity.
Protein Sci., 29:2387-2397, 2020

PubMed Abstract: During adaptive metabolic evolution a native glycerol dehydrogenase (GDH) acquired a d-lactate dehydrogenase (LDH) activity. Two active-site amino acid changes were detected in the altered protein. Biochemical studies along with comparative structure analysis using an X-ray crystallographic structure model of the protein with the two different amino acids allowed prediction of pyruvate binding into the active site. We propose that the F245S alteration increased the capacity of the glycerol binding site and facilitated hydrogen bonding between the S245 γ-O and the C1 carboxylate of pyruvate. To our knowledge, this is the first GDH to gain LDH activity due to an active site amino acid change, a desired result of in vivo enzyme evolution.

PubMed: 33020946
DOI: 10.1002/pro.3963

実験手法

X-RAY DIFFRACTION (2.395 Å)