1UP8

Recombinant vanadium-dependent bromoperoxidase from red algae Corallina pilulifera

1UP8 の概要

• エントリーDOI: 10.2210/pdb1up8/pdb
• 分子名称: VANADIUM-DEPENDENT BROMOPEROXIDASE 1, PHOSPHATE ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: haloperoxidase, vanadate
• 由来する生物種: CORALLINA PILULIFERA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 263055.64

構造登録者

Garcia-Rodriguez, E.,Isupov, M.,Ohshiro, T.,Izumi, Y.,Littlechild, J.A. (登録日: 2003-09-29, 公開日: 2003-09-30, 最終更新日: 2023-12-13)

主引用文献

Garcia-Rodriguez, E.,Ohshiro, T.,Aibara, T.,Izumi, Y.,Littlechild, J.
Enhancing Effect of Calcium and Vanadium Ions on Thermal Stability of Bromoperoxidase from Corallina Pilulifera.
J.Biol.Inorg.Chem., 10:275-, 2005

PubMed Abstract: Bromoperoxidase from the macro-alga Corallina pilulifera is an enzyme that possesses vanadate in the catalytic center, and shows a significant thermostability and stability toward organic solvents. The structural analysis of the recombinant enzyme overexpressed in yeast revealed that it contains one calcium atom per subunit. This has been confirmed by inductively coupled plasma emission spectrometry experiments. The study of the effect of metal ions on the apo-enzyme stability has shown that the calcium ion significantly increased the enzyme stability. In addition, vanadate also increased the thermostability and strontium and magnesium ions had similar effects as calcium. The holo-enzyme shows high stability in a range of organic solvents. The effect of the different ions and solvents on the structure of the enzyme has been studied by circular dichroism experiments. The high stability of the enzyme in the presence of organic solvents is useful for its application as a biocatalyst.

PubMed: 15776268
DOI: 10.1007/S00775-005-0639-3

実験手法

X-RAY DIFFRACTION (2.2 Å)