4HD7

Crystal Structure of Tyrosinase from Bacillus megaterium V218G mutant soaked in CuSO4

4HD7 の概要

• エントリーDOI: 10.2210/pdb4hd7/pdb
• 関連するPDBエントリー: 4HD4 4HD6 4HDA
• 分子名称: Tyrosinase, COPPER (II) ION (3 entities in total)
• 機能のキーワード: tyrosinase, type 3 copper protein, oxidoreductase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70678.97

構造登録者

Goldfeder, M.,Kanteev, M.,Adir, N.,Fishman, A. (登録日: 2012-10-02, 公開日: 2013-01-23, 最終更新日: 2024-02-28)

主引用文献

Goldfeder, M.,Kanteev, M.,Adir, N.,Fishman, A.
Influencing the monophenolase/diphenolase activity ratio in tyrosinase.
Biochim.Biophys.Acta, 1834:629-633, 2013

PubMed Abstract: Tyrosinase is a type 3 copper enzyme with great potential for production of commercially valuable diphenols from monophenols. However, the use of tyrosinase is limited by its further oxidation of diphenols to quinones. We recently determined the structure of the Bacillus megaterium tyrosinase revealing a residue, V218, which we proposed to take part in positioning of substrates within the active site. In the structure of catechol oxidase from Ipomoea batatas, the lack of monophenolase activity was attributed to the presence of F261 near CuA. Consequently, we engineered two variants, V218F and V218G. V218F was expected to have a decreased monophenolase activity, due to the bulky residue extending into the active site. Surprisingly, both V218F and V218G exhibited a 9- and 4.4-fold higher monophenolase/diphenolase activity ratio, respectively. X-ray structures of variant V218F display a flexibility of the phenylalanine residue along with an adjacent histidine, which we propose to be the source of the change in activity ratio.

PubMed: 23305929
DOI: 10.1016/j.bbapap.2012.12.021

実験手法

X-RAY DIFFRACTION (2.1 Å)