6JJS

Crystal structure of an enzyme from Penicillium herquei in condition2

6JJS の概要

• エントリーDOI: 10.2210/pdb6jjs/pdb
• 分子名称: PhnH, ACETATE ION (3 entities in total)
• 機能のキーワード: prenyltransferase, transferase
• 由来する生物種: Penicillium herquei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16282.08

構造登録者

Fen, Y.,Huang, J.W.,Liu, W.D.,Chen, C.C.,Guo, R.T. (登録日: 2019-02-26, 公開日: 2020-01-01, 最終更新日: 2023-11-22)

主引用文献

Feng, Y.,Yu, X.,Huang, J.W.,Liu, W.,Li, Q.,Hu, Y.,Yang, Y.,Chen, Y.,Jin, J.,Li, H.,Chen, C.C.,Guo, R.T.
Crystal structure and proposed mechanism of an enantioselective hydroalkoxylation enzyme from Penicillium herquei.
Biochem.Biophys.Res.Commun., 516:801-805, 2019

PubMed Abstract: Hydroalkoxylation is a useful and efficient reaction which generates C-O bond and produces cyclic ethers, the common structural elements of natural products. The dedicative enzyme which can catalyze enantioselective hydroalkoxylation named PhnH was recently identified in the herqueinone biosynthetic gene from Penicillium herquei. It catalyzes addition of a phenol to the terminal olefin on substrate to produce a dihydrobenzofuran. Here, the crystal structure of PhnH is reported and the putative substrate-binding pocket is illustrated. Through docking experiment, possible substrate-binding poses are displayed and the catalytic mechanism is therefore proposed. Our findings form the basis for further studies of enantioselective hydroalkoxylation enzymes.

PubMed: 31256936
DOI: 10.1016/j.bbrc.2019.06.100

実験手法

X-RAY DIFFRACTION (1.62 Å)