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

More general terms

• oxidoreductase
• flavoprotein

Database

• UniProt: http://www.uniprot.org/uniprot/P00390.html
• OMIM: https://mirror.omim.org/entry/138300