6VPD

Crystal structure of Trgpx in apo form

6VPD の概要

• エントリーDOI: 10.2210/pdb6vpd/pdb
• 分子名称: Glutathione peroxidase (2 entities in total)
• 機能のキーワード: glutathione peroxidase, oxidoreductase
• 由来する生物種: Hypocrea jecorina (strain QM6a)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44394.61

構造登録者

Adriani, P.P.,De Oliveira, G.S.,Paiva, F.C.R.,Dias, M.V.B.,Chambergo, F.S. (登録日: 2020-02-03, 公開日: 2020-12-16, 最終更新日: 2023-10-11)

主引用文献

Adriani, P.P.,de Paiva, F.C.R.,de Oliveira, G.S.,Leite, A.C.,Sanches, A.S.,Lopes, A.R.,Dias, M.V.B.,Chambergo, F.S.
Structural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reesei.
Int.J.Biol.Macromol., 167:93-100, 2020

PubMed Abstract: Glutathione peroxidases (GPx) are a family of enzymes with the ability to reduce organic and inorganic hydroperoxides to the corresponding alcohols using glutathione or thioredoxin as an electron donor. Here, we report the functional and structural characterization of a GPx identified in Trichoderma reesei (TrGPx). TrGPx was recombinantly expressed in a bacterial host and purified using affinity. Using a thioredoxin coupled assay, TrGPx exhibited activity of 28 U and 12.5 U in the presence of the substrates HO and t-BOOH, respectively, and no activity was observed when glutathione was used. These results indicated that TrGPx is a thioredoxin peroxidase and hydrolyses HO better than t-BOOH. TrGPx kinetic parameters using a pyrogallol assay resulted at K = 11.7 mM V = 10.9 IU/μg TrGPx, k = 19 s and a catalytic efficiency of 1.6 mM s to HO as substrate. Besides that, TrGPx demonstrated an optimum pH ranging from 9.0-12.0 and a half-life of 36 min at 80 °C. TrGPx 3D-structure was obtained in a reduced state and non-catalytic conformation. The overall fold is similar to the other phospholipid-hydroperoxide glutathione peroxidases. These data contribute to understand the antioxidant mechanism in fungi and provide information for using antioxidant enzymes in biotechnological applications.

PubMed: 33259843
DOI: 10.1016/j.ijbiomac.2020.11.179

実験手法

X-RAY DIFFRACTION (2.603 Å)