Sandbox 181
From Proteopedia
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== Structure == | == Structure == | ||
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| + | Glutathione reductase belongs to the larger family of [[flavoezymes]], which use a [[flavin adenine dinucleotide]] (FAD) or [[flavin mononucleotide]] (FMN) in catalysis. It is an oxiodrecutase homodimer of 52kD monomers of which, each has three domains: | ||
| + | 1. NADPH-binding domain, | ||
| + | 2. FAD-binding domain, | ||
| + | 3. dimerization domain. | ||
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| + | == Reaction == | ||
| + | The action of glutathione reductase proceeds through a cyclic series of structures in differing redox states (Figure 1). Initiating the reduction, NADPH binds to glutathione reductase to transiently reduce the flavin co-factor. By forming a transient covalent | ||
| + | |||
Revision as of 23:54, 18 March 2010
Glutathione reductase, also known as GSH reductase, converts oxidized glutathione (glutathione disulfide) to two molecules of reduced gluthatione (GSH).
Structure
Glutathione reductase belongs to the larger family of flavoezymes, which use a flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) in catalysis. It is an oxiodrecutase homodimer of 52kD monomers of which, each has three domains: 1. NADPH-binding domain, 2. FAD-binding domain, 3. dimerization domain.
Reaction
The action of glutathione reductase proceeds through a cyclic series of structures in differing redox states (Figure 1). Initiating the reduction, NADPH binds to glutathione reductase to transiently reduce the flavin co-factor. By forming a transient covalent
Human Glutathione Reductase
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
