Peroxiredoxin HYR1 (P40581)

Identification
NamePeroxiredoxin HYR1
Synonyms
  • Glutathione peroxidase 3
  • Hydrogen peroxide resistance protein 1
  • Oxidant receptor peroxidase 1
  • Phospholipid hydroperoxide glutathione peroxidase 3
  • PHGPx3
Gene NameHYR1
Enzyme Class
Biological Properties
General FunctionInvolved in glutathione peroxidase activity
Specific FunctionInvolved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYP1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYP1 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598') and a reduced Cys-36 in HYP1/GPX3
Cellular LocationCytoplasm
SMPDB Pathways
Glutathione metabolismPW002395 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glutathione metabolismec00480 Map00480
SMPDB ReactionsNot Available
KEGG Reactions
Hydrogen peroxide + Glutathione ↔ water + Oxidized glutathione
Metabolites
YMDB IDNameView
YMDB00057Oxidized glutathioneShow
YMDB00160GlutathioneShow
YMDB00693glutathione disulfideShow
YMDB00888Hydrogen peroxideShow
YMDB00890waterShow
GO Classification
Component
Not Available
Function
antioxidant activity
peroxidase activity
glutathione peroxidase activity
Process
response to oxidative stress
metabolic process
oxidation reduction
response to stimulus
response to stress
Gene Properties
Chromosome Locationchromosome 9
LocusYIR037W
Gene Sequence>492 bp ATGTCAGAATTCTATAAGCTAGCACCTGTTGACAAGAAAGGCCAACCATTCCCCTTCGAC CAATTAAAGGGAAAAGTGGTGCTTATCGTTAATGTTGCCTCCAAATGTGGATTCACTCCT CAATACAAAGAACTAGAGGCCTTGTACAAACGTTATAAGGACGAAGGATTTACCATCATC GGGTTCCCATGCAACCAGTTTGGCCACCAAGAACCTGGCTCTGATGAAGAAATTGCCCAG TTCTGCCAACTGAACTATGGCGTGACTTTCCCCATTATGAAAAAAATTGACGTTAATGGT GGCAATGAGGACCCTGTTTACAAGTTTTTGAAGAGCCAAAAATCCGGTATGTTGGGCTTG AGAGGTATCAAATGGAATTTTGAAAAATTCTTAGTCGATAAAAAGGGTAAAGTGTACGAA AGATACTCTTCACTAACCAAACCTTCTTCGTTGTCCGAAACCATCGAAGAACTTTTGAAA GAGGTGGAATAG
Protein Properties
Pfam Domain Function
Protein Residues163
Protein Molecular Weight18641.40039
Protein Theoretical pI8.42
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Peroxiredoxin HYR1 MSEFYKLAPVDKKGQPFPFDQLKGKVVLIVNVASKCGFTPQYKELEALYKRYKDEGFTII GFPCNQFGHQEPGSDEEIAQFCQLNYGVTFPIMKKIDVNGGNEDPVYKFLKSQKSGMLGL RGIKWNFEKFLVDKKGKVYERYSSLTKPSSLSETIEELLKEVE
References
External Links
ResourceLink
Saccharomyces Genome Database HYR1
Uniprot IDP40581
Uniprot NameGPX3_YEAST
GenBank Gene IDU22446
Genebank Protein ID727367
General Reference
  • Avery, A. M., Avery, S. V. (2001). "Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases." J Biol Chem 276:33730-33735.11445588
  • Veal, E. A., Ross, S. J., Malakasi, P., Peacock, E., Morgan, B. A. (2003). "Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor." J Biol Chem 278:30896-30904.12743123
  • Delaunay, A., Pflieger, D., Barrault, M. B., Vinh, J., Toledano, M. B. (2002). "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation." Cell 111:471-481.12437921
  • Wood, Z. A., Schroder, E., Robin Harris, J., Poole, L. B. (2003). "Structure, mechanism and regulation of peroxiredoxins." Trends Biochem Sci 28:32-40.12517450
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • 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
  • Zhang, W. J., He, Y. X., Yang, Z., Yu, J., Chen, Y., Zhou, C. Z. (2008). "Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae." Proteins 73:1058-1062.18767166
  • Inoue, Y., Matsuda, T., Sugiyama, K., Izawa, S., Kimura, A. (1999). "Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae." J Biol Chem 274:27002-27009.10480913
  • 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
  • Azevedo, D., Tacnet, F., Delaunay, A., Rodrigues-Pousada, C., Toledano, M. B. (2003). "Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling." Free Radic Biol Med 35:889-900.14556853
  • Ursini, F., Maiorino, M., Roveri, A. (1997). "Phospholipid hydroperoxide glutathione peroxidase (PHGPx): more than an antioxidant enzyme?" Biomed Environ Sci 10:327-332.9315326
  • Carmel-Harel, O., Storz, G. (2000). "Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and saccharomyces cerevisiae responses to oxidative stress." Annu Rev Microbiol 54:439-461.11018134