Sandbox 181: Difference between revisions
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Glutathione reductase, also known as GSH reductase, is found in the human cells and converts oxidized glutathione (GSSG) to two molecules of reduced [[gluthatione]] (GSH) <ref name="main">PMID:18638483</ref>. EC:[http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/8/1/7.html 1.8.1.7] | Glutathione reductase, also known as GSH reductase, is found in the human cells and converts oxidized glutathione (GSSG) to two molecules of reduced [[gluthatione]] (GSH) <ref name="main">PMID:18638483</ref>. EC:[http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/8/1/7.html 1.8.1.7] | ||
{{STRUCTURE_3djj| PDB=3djj |SCENE=Sandbox_181/Cpk_default/1}} | {{STRUCTURE_3djj| PDB=3djj |SCENE=Sandbox_181/Cpk_default/1}} | ||
= | =Overview= | ||
Glutathione reductase belongs to the larger family of [[flavoezymes]], which use a [[flavin adenine dinucleotide]] (FAD) or [[flavin mononucleotide]] (FMN) in catalysis. It is a disulfide oxiodreductase homodimer of 52kD monomers of which, each has three domains: | Glutathione reductase belongs to the larger family of [[flavoezymes]], which use a [[flavin adenine dinucleotide]] (FAD) or [[flavin mononucleotide]] (FMN) in catalysis. It is a disulfide oxiodreductase homodimer of 52kD monomers of which, each has three domains: | ||
(<scene name='Sandbox_181/Fad_ndp_highlight/1'>FAD and NADPH Highlighted</scene>) | (<scene name='Sandbox_181/Fad_ndp_highlight/1'>FAD and NADPH Highlighted</scene>) | ||
1. NADPH-binding domain (yellow), | 1. NADPH-binding domain (yellow), | ||
2. FAD-binding domain (red), | 2. FAD-binding domain (red), | ||
3. dimerization domain. | 3. dimerization domain. | ||
It is a thermostable protein as it retains 100% of its function up to 65 degrees Celsius attributing to the importance of its function in the cell <ref>PMID: 2044390</ref>. | |||
==Topology== | ==Topology== | ||
GSH reductase has a central five-stranded parallel beta-sheet (beta1, beta2, beta3, beta7 and beta8) <ref name="Dym">PMID:11514662</ref>. This central beta-sheet is surrounded by alpha-helices 1 and 2 with another crossover connection of a three-stranded antiparallel beta-sheet (beta4-6). | GSH reductase has a central five-stranded parallel beta-sheet (beta1, beta2, beta3, beta7 and beta8) <ref name="Dym">PMID:11514662</ref>. This central beta-sheet is surrounded by alpha-helices 1 and 2 with another crossover connection of a three-stranded antiparallel beta-sheet (beta4-6). | ||
