Member database | NCBIfam (includes TIGRFAMs) |
NCBIfam type | family |
Short name | GRXB |
Description
Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [1]. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase [2], and may have more to do with resistance to redox stress [3].
References
1. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Fernandes AP, Holmgren A. Antioxid. Redox Signal. 6, 63-74, (2004). View articlePMID: 14713336
2. Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli. Ortenberg R, Gon S, Porat A, Beckwith J. Proc. Natl. Acad. Sci. U.S.A. 101, 7439-44, (2004). View articlePMID: 15123823
3. Characterization of Escherichia coli null mutants for glutaredoxin 2. Vlamis-Gardikas A, Potamitou A, Zarivach R, Hochman A, Holmgren A. J. Biol. Chem. 277, 10861-8, (2002). View articlePMID: 11741965
Integrated to
External Links
Representative structure
7dkp: Crystal structure of E. coli Grx2 in complex with GSH at 1.45 A resolution