4YAR

2-Hydroxyethylphosphonate dioxygenase (HEPD) E176H

4YAR の概要

• エントリーDOI: 10.2210/pdb4yar/pdb
• 分子名称: 2-hydroxyethylphosphonate dioxygenase, CADMIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: dioxygenase, oxidoreductase
• 由来する生物種: Streptomyces viridochromogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49422.56

構造登録者

Chekan, J.R.,Nair, S.K. (登録日: 2015-02-17, 公開日: 2015-03-04, 最終更新日: 2023-09-27)

主引用文献

Peck, S.C.,Chekan, J.R.,Ulrich, E.C.,Nair, S.K.,van der Donk, W.A.
A Common Late-Stage Intermediate in Catalysis by 2-Hydroxyethyl-phosphonate Dioxygenase and Methylphosphonate Synthase.
J.Am.Chem.Soc., 137:3217-3220, 2015

PubMed Abstract: 2-Hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS) are nonheme iron oxygenases that both catalyze the carbon-carbon bond cleavage of 2-hydroxyethylphosphonate but generate different products. Substrate labeling experiments led to a mechanistic hypothesis in which the fate of a common intermediate determined product identity. We report here the generation of a bifunctional mutant of HEPD (E176H) that exhibits the activity of both HEPD and MPnS. The product distribution of the mutant is sensitive to a substrate isotope effect, consistent with an isotope-sensitive branching mechanism involving a common intermediate. The X-ray structure of the mutant was determined and suggested that the introduced histidine does not coordinate the active site metal, unlike the iron-binding glutamate it replaced.

PubMed: 25699631
DOI: 10.1021/jacs.5b00282

実験手法

X-RAY DIFFRACTION (1.75 Å)