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Identification
NameGlutaredoxin-1
Synonyms
  • Glutathione-dependent oxidoreductase 1
Gene NameGRX1
Enzyme ClassNot Available
Biological Properties
General FunctionInvolved in electron carrier activity
Specific FunctionMultifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S- transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
Hydrogen peroxide + Glutathionewater + Oxidized glutathione
Metabolites
YMDB IDNameView
YMDB00057Oxidized glutathioneShow
YMDB00160GlutathioneShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00693glutathione disulfideShow
YMDB00862hydronShow
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
catalytic activity
oxidoreductase activity
electron carrier activity
oxidoreductase activity, acting on a sulfur group of donors
Process
cellular process
cellular homeostasis
cell redox homeostasis
Gene Properties
Chromosome Locationchromosome 3
LocusYCL035C
Gene Sequence>333 bp ATGGTATCTCAAGAAACTATCAAGCACGTCAAGGACCTTATTGCAGAAAACGAGATCTTC GTCGCATCCAAAACGTACTGTCCATACTGCCATGCAGCCCTAAACACGCTTTTTGAAAAG TTAAAGGTTCCCAGGTCCAAAGTTCTGGTTTTGCAATTGAATGACATGAAGGAAGGCGCA GACATTCAGGCTGCGTTATATGAGATTAATGGCCAAAGAACCGTGCCAAACATCTATATT AATGGTAAACATATTGGAGGCAACGACGACTTGCAGGAATTGAGGGAGACTGGTGAATTG GAGGAATTGTTAGAACCTATTCTTGCAAATTAA
Protein Properties
Pfam Domain Function
Protein Residues110
Protein Molecular Weight12380.09961
Protein Theoretical pI4.72
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glutaredoxin-1 MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGA DIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN
References
External Links
ResourceLink
Saccharomyces Genome Database GRX1
Uniprot IDP25373
Uniprot NameGLRX1_YEAST
GenBank Gene IDX59720
Genebank Protein ID5328
General Reference
  • Oliver, S. G., van der Aart, Q. J., Agostoni-Carbone, M. L., Aigle, M., Alberghina, L., Alexandraki, D., Antoine, G., Anwar, R., Ballesta, J. P., Benit, P., et, a. l. .. (1992). "The complete DNA sequence of yeast chromosome III." Nature 357:38-46.1574125
  • Luikenhuis, S., Perrone, G., Dawes, I. W., Grant, C. M. (1998). "The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species." Mol Biol Cell 9:1081-1091.9571241
  • Grant, C. M., Luikenhuis, S., Beckhouse, A., Soderbergh, M., Dawes, I. W. (2000). "Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae." Biochim Biophys Acta 1490:33-42.10786615
  • Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., Grant, C. M. (2002). "The yeast glutaredoxins are active as glutathione peroxidases." J Biol Chem 277:16712-16717.11875065
  • Collinson, E. J., Grant, C. M. (2003). "Role of yeast glutaredoxins as glutathione S-transferases." J Biol Chem 278:22492-22497.12684511
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106