6AH7

D45W/H226G mutant of marine bacterial prolidase

6AH7 の概要

• エントリーDOI: 10.2210/pdb6ah7/pdb
• 分子名称: Xaa-Pro dipeptidase, MANGANESE (II) ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: paraoxonase, hydrolase
• 由来する生物種: Pseudoalteromonas lipolytica
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 207075.21

構造登録者

Jian, Y.,Yunzhu, X.,Lijuan, L. (登録日: 2018-08-17, 公開日: 2019-09-18, 最終更新日: 2023-11-22)

主引用文献

Yang, J.,Xiao, Y.Z.,Li, R.,Liu, Y.,Long, L.J.
Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity.
Biotechnol.Bioeng., 117:2694-2702, 2020

PubMed Abstract: Enzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions.

PubMed: 32515491
DOI: 10.1002/bit.27455

実験手法

X-RAY DIFFRACTION (2.38 Å)