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glutathione reductase (GSR)
Function:
- maintains high levels of reduced glutathione in cytosol
2 glutathione + NADP+ glutathione disulfide + NADPH
Cofactor: binds 1 FAD per subunit
Structure:
- homodimer; disulfide-linked
- initiator Met-1 of isoform cytoplasmic is removed
- contains a N-acetylalanine at position 2
- each subunit can be divided into 4 domains that are consecutive along the polypeptide chain
- omains 1 & 2 bind FAD & NADPH, respectively
- domain 4 forms the interface
- belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family
- active site is a redox-active disulfide bond
Compartment: mitochondria, cytoplasm
Alternative initiation: Named isoforms=2
Laboratory:
- glutathione reductase in erythrocytes
Related
glutathione reductase deficiency
glutathione reductase in erythrocytes
General
flavoprotein
oxidoreductase
Properties
MOTIF: active site
MOTIF: cofactor-binding site
COFACTOR-BOUND: reduced flavin adenine dinucleotide
cysteine residue (2)
Database Correlations
OMIM 138300
UniProt P00390
ENZYME 1.6.4.2
References
- UniProt :accession P00390
- Wikipedia; Note: Glutathione reductase entry
http://en.wikipedia.org/wiki/Glutathione_reductase