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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
oxidoreductase activity, acting on a sulfur group of donors
disulfide oxidoreductase activity
protein disulfide oxidoreductase activity
catalytic activity
oxidoreductase activity
electron carrier activity
Process
cell redox homeostasis
cellular process
cellular 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