5LPC

Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

5LPC の概要

• エントリーDOI: 10.2210/pdb5lpc/pdb
• 関連するPDBエントリー: 1UP8
• 分子名称: Vanadium-dependent bromoperoxidase, PHOSPHATE ION (2 entities in total)
• 機能のキーワード: vanadium, enzyme catalysis, peroxidase, halogenation, oxidoreductase
• 由来する生物種: Acaryochloris marina
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 73164.59

構造登録者

Frank, A.,Groll, M. (登録日: 2016-08-12, 公開日: 2016-08-24, 最終更新日: 2024-11-13)

主引用文献

Frank, A.,Seel, C.J.,Groll, M.,Gulder, T.
Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.
Chembiochem, 17:2028-2032, 2016

PubMed Abstract: Vanadium-dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina (AmVHPO), including its structure determination by X-ray crystallography. Compared to other VHPOs, the AmVHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high-yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.

PubMed: 27542168
DOI: 10.1002/cbic.201600417

実験手法

X-RAY DIFFRACTION (3.1 Å)