2487-09-4
Chemical Structure
GSeSeG
Synonym(s): Glutaselenone diselenide
- CAS No.: 2487-09-4
- Formula:C20H32N6O12Se2
- Molecular Weight:706.42
InChIKey: QLLZDMKEQUBHQO-BJDJZHNGSA-N
SMILES: OC([C@@H](N)CCC(N[C@@H](C[Se][Se]C[C@@H](C(NCC(O)=O)=O)NC(CC[C@H](N)C(O)=O)=O)C(NCC(O)=O)=O)=O)=O
Biological Activity: GSeSeG (Glutaselenone diselenide) is the oxidized diselenide form of selenoglutathione (GSeH), a selenium analog of glutathione in which selenocysteine replaces cysteine. GSeSeG serves as a substrate for Glutathione Reductase (GR) with a Km of 54 μM. GSeSeG is reduced by the GR/NADPH system to generate GSeH. GSeSeG also promotes the oxidative folding of disulfide-containing proteins and the rearrangement of incorrect disulfide bonds. GSeSeG is used in studies of redox regulation, oxidative/glycation stress, and protein folding[1][2][3][4].
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GSeSeG | GSeSeG (Glutaselenone diselenide) is the oxidized diselenide form of selenoglutathione (GSeH), a selenium analog of glutathione in which selenocysteine replaces cysteine. GSeSeG serves as a substrate for Glutathione Reductase (GR) with a Km of 54 μM. GSeSeG is reduced by the GR/NADPH system to generate GSeH. GSeSeG also promotes the oxidative folding of disulfide-containing proteins and the rearrangement of incorrect disulfide bonds. GSeSeG is used in studies of redox regulation, oxidative/glycation stress, and protein folding. | |||||||||||||||||||||
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References
- [1]. Iwaoka M. A Selenium Analog of Glutathione. Synthesis and Applications. Metallomics Research. 2024 Nov 30;4(3):rev01-13.
- [2]. Beld J, et al. Selenoglutathione: efficient oxidative protein folding by a diselenide. Biochemistry. 2007 May 08;46(18):5382-90.
- [3]. Kanamori A, et al. Antioxidative and Antiglycative Stress Activities of Selenoglutathione Diselenide. Pharmaceuticals (Basel, Switzerland). 2024 Aug 09;17(8):1049.
- [4]. Shimodaira S, et al. Selenoglutathione Diselenide: Unique Redox Reactions in the GPx-Like Catalytic Cycle and Repairing of Disulfide Bonds in Scrambled Protein. Biochemistry. 2017 Oct 24;56(42):5644-5653.
