Glutathione peroxidase

Base Information

• Chemical Name: Glutathione peroxidase
• CAS No.: 9013-66-5
• Molecular Formula: NULL
• Molecular Weight: 0
• Mol file: 9013-66-5.mol

Synonyms:E.C.1.11.1.9;GSH peroxidase;Glutathione sulfhydrylperoxidase;Peroxynitrite reductase;Reduced glutathione peroxidase;Peroxidase, glutathione;

Chemical Property of Glutathione peroxidase

Chemical Property:

• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: −20°C

Purity/Quality:

98%,99%, ^*data from raw suppliers

Glutathione Peroxidase ^*data from reagent suppliers

Safty Information:

• Hazard Codes: B,Xi
• Statements: 36/37/38
• Safety Statements: 22-24/25-36-26

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• General Description: Glutathione peroxidase (GPx), also known as GSH peroxidase, glutathione sulfhydrylperoxidase, or peroxynitrite reductase, is a critical antioxidant enzyme that protects cells from oxidative damage by catalyzing the reduction of hydroperoxides using glutathione (GSH) as a reducing agent. The enzyme's activity is influenced by steric and electronic factors, as demonstrated by studies on synthetic mimics, where substituent positioning (e.g., methoxy groups) can either enhance catalytic efficiency by preventing side reactions or improve electron donation to stabilize reactive intermediates. These insights aid in designing more effective GPx-like antioxidants.

Refernces

Tertiary amine-based glutathione peroxidase mimics: Some insights into the role of steric and electronic effects on antioxidant activity

10.1016/j.tet.2012.09.020

The study investigates the role of steric and electronic effects on the antioxidant activity of tertiary amine-based diaryl diselenides, which mimic the function of glutathione peroxidase (GPx). The researchers synthesized various diselenides with methoxy substituents at different positions and evaluated their GPx-like activities using hydrogen peroxide, tert-butyl hydroperoxide, and cumene hydroperoxide as substrates, with thiophenol (PhSH) and glutathione (GSH) as co-substrates. The findings indicate that the position of the methoxy substituent significantly influences the catalytic activity. Specifically, the 6-methoxy substituent provides steric protection, preventing undesired thiol exchange reactions and the formation of seleninic and selenonic acids, thereby enhancing GPx-like activity. In contrast, the 4-methoxy substituent enhances activity when GSH is used as the co-substrate, likely due to its electronic effects. The study provides insights into the design of more effective GPx mimics by understanding the impact of substituent positions on the catalytic cycle and reactivity of these compounds.

Biotransformation of benzoin by Sphingomonas sp. LK11 and ameliorative effects on growth of Cucumis sativus

10.1007/s00203-019-01623-1

The research investigates the biotransformation of benzoin to benzamide by the plant endophyte Sphingomonas sp. LK11 and its effects on the growth and stress tolerance of Cucumis sativus (cucumber). The study found that Sphingomonas sp. LK11 can convert benzoin to benzamide, which acts as an abiotic stress agent when applied to cucumber plants, reducing their agronomic potential. However, when the plants were inoculated with Sphingomonas sp. LK11 along with benzamide, the negative effects were mitigated, and the plants' growth and stress tolerance were improved. The inoculated plants showed higher levels of chlorophyll b and carotenoids, indicating enhanced photosynthetic capacity and stress tolerance. The study also revealed that Sphingomonas sp. LK11 could regulate oxidative stress by reducing the levels of peroxidase, catalase, and glutathione peroxidase in benzamide-treated plants. The findings suggest that Sphingomonas sp. LK11 has potential for plant growth promotion and stress tolerance through its biotransformation capabilities and its ability to modulate plant physiological processes.