EzCatDB: S00279

DB codeS00279
CATH domainDomain 13.40.30.10Catalytic domain
E.C.1.11.1.9
CSA1gp1

CATH domainRelated DB codes (homologues)
3.40.30.10S00916,M00184,D00866,D00869,D00870,D00278

Enzyme Name
Swiss-protKEGG

P00435
Protein nameGlutathione peroxidase 1glutathione peroxidase
GSH peroxidase
selenium-glutathione peroxidase
reduced glutathione peroxidase
SynonymsEC 1.11.1.9
GSHPx-1
GPx-1
Cellular glutathione peroxidase

KEGG pathways
MAP codePathways
MAP00480Glutathione metabolism
MAP00590Arachidonic acid metabolism

Swiss-prot:Accession NumberP00435
Entry nameGPX1_BOVIN
Activity2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O.
SubunitHomotetramer.
Subcellular locationCytoplasm.
Cofactor


CofactorsSubstratesProducts
KEGG-idC01529C00051C00027C00127C00001
CompoundSeleniumGlutathioneH2O2Oxidized glutathioneH2O
Typeothersamino acids,carboxyl group,peptide/protein,sulfhydryl groupothersamino acids,carboxyl group,peptide/protein,disulfide bondH2O
1gp1ABound:SECUnboundUnboundUnbound
1gp1BBound:SECUnboundUnboundUnbound

Active-site residues
pdbModified residues
1gp1ASEC 45(Seleninic acid)
1gp1BSEC 45(Seleninic acid)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.66-68, Fig.13
[6]Fig.1, p.304
[7]p.216-218
[8]p.90-91
[9]p.147-149
[10]p.878-880

references
[1]
PubMed ID1140308
JournalExperientia
Year1975
Volume31
Pages769-70
AuthorsBeutler E, Beutler B, Matsumoto J
TitleGlutathione peroxidase activity of inorganic selenium and seleno-DL-cysteine.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID83209650
PubMed ID6852035
JournalEur J Biochem
Year1983
Volume133
Pages51-69
AuthorsEpp O, Ladenstein R, Wendel A
TitleThe refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.
Related PDB1gp1
Related Swiss-protP00435
[3]
PubMed ID6714945
JournalHoppe Seylers Z Physiol Chem
Year1984
Volume365
Pages195-212
AuthorsGunzler WA, Steffens GJ, Grossmann A, Kim SM, Otting F, Wendel A, Flohe L
TitleThe amino-acid sequence of bovine glutathione peroxidase.
[4]
PubMed ID6233508
JournalNutr Rev
Year1984
Volume42
Pages168-9
Authors[No authors listed]
TitlePosition and function of the organic selenium in glutathione peroxidase.
[5]
PubMed ID2130181
JournalJ Toxicol Clin Exp
Year1990
Volume10
Pages375-83
AuthorsBompart G
TitleCisplatin-induced changes on cytochrome P-450, lipid peroxidation and some P-450 related specific catalytic activities in rat liver.
[6]
PubMed ID7651210
JournalMethods Enzymol
Year1995
Volume251
Pages303-14
AuthorsBiewenga GP, Bast A
TitleReaction of lipoic acid with ebselen and hypochlorous acid.
[7]
PubMed ID7766257
JournalZ Naturforsch [C]
Year1995
Volume50
Pages209-19
AuthorsPrutz WA
TitleGlutathione peroxidase-like activity of simple selenium compounds. Peroxides and the heterocyclic N-oxide resazurin acting as O-atom donors.
[8]
PubMed ID8912640
JournalBiochem Biophys Res Commun
Year1996
Volume228
Pages88-93
AuthorsHou Y, Guo Z, Li J, Wang PG
TitleSeleno compounds and glutathione peroxidase catalyzed decomposition of S-nitrosothiols.
[9]
PubMed ID9315305
JournalBiomed Environ Sci
Year1997
Volume10
Pages136-55
AuthorsAumann KD, Bedorf N, Brigelius-Flohe R, Schomburg D, Flohe L
TitleGlutathione peroxidase revisited--simulation of the catalytic cycle by computer-assisted molecular modelling.
[10]
PubMed ID9180378
JournalJ Mol Biol
Year1997
Volume268
Pages869-85
AuthorsRen B, Huang W, Akesson B, Ladenstein R
TitleThe crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 A resolution.
[11]
PubMed ID9517485
JournalBiol Trace Elem Res
Year1998
Volume61
Pages127-36
AuthorsHoward SA, Hawkes WC
TitleThe relative effectiveness of human plasma glutathione peroxidase as a catalyst for the reduction of hydroperoxides by glutathione.
[12]
PubMed ID9828014
JournalProtein Sci
Year1998
Volume7
Pages2465-8
AuthorsSchroder E, Ponting CP
TitleEvidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
[13]
PubMed ID11018712
JournalBiochim Biophys Acta
Year2000
Volume1481
Pages222-8
AuthorsLiu J, Luo G, Ren X, Mu Y, Bai Y, Shen J
TitleA bis-cyclodextrin diselenide with glutathione peroxidase-like activity.
[14]
PubMed ID10995212
JournalBioconjug Chem
Year2000
Volume11
Pages682-7
AuthorsRen X, Liu J, Luo G, Zhang Y, Luo Y, Yan G, Shen J
TitleA novel selenocystine-beta-cyclodextrin conjugate that acts as a glutathione peroxidase mimic.
[15]
PubMed ID11697854
JournalArch Biochem Biophys
Year2001
Volume395
Pages177-84
AuthorsSu D, Ren X, You D, Li D, Mu Y, Yan G, Zhang Y, Luo Y, Xue Y, Shen J, Liu Z, Luo G
TitleGeneration of three selenium-containing catalytic antibodies with high catalytic efficiency using a novel hapten design method.
[16]
PubMed ID11485327
JournalBiochem Biophys Res Commun
Year2001
Volume286
Pages189-94
AuthorsSu D, You D, Ren X, Luo G, Mu Y, Yan G, Xue Y, Shen J
TitleKinetics study of a selenium-containing ScFv catalytic antibody that mimics glutathione peroxidase.
[17]
PubMed ID11456617
JournalJ Am Chem Soc
Year2001
Volume123
Pages839-50
AuthorsMugesh G, Panda A, Singh HB, Punekar NS, Butcher RJ
TitleGlutathione peroxidase-like antioxidant activity of diaryl diselenides: a mechanistic study.
[18]
PubMed ID11678710
JournalOrg Lett
Year2001
Volume3
Pages3569-72
AuthorsGoto K, Nagahama M, Mizushima T, Shimada K, Kawashima T, Okazaki R
TitleThe first direct oxidative conversion of a selenol to a stable selenenic acid: experimental demonstration of three processes included in the catalytic cycle of glutathione peroxidase.
[19]
PubMed ID12371844
JournalJ Am Chem Soc
Year2002
Volume124
Pages12104-5
AuthorsBack TG, Moussa Z
TitleRemarkable activity of a novel cyclic seleninate ester as a glutathione peroxidase mimetic and its facile in situ generation from allyl 3-hydroxypropyl selenide.
[20]
PubMed ID11996219
JournalJ Biotechnol
Year2002
Volume82
Pages411-24
AuthorsScheller FW, Wollenberger U, Lei C, Jin W, Ge B, Lehmann C, Lisdat F, Fridman V
TitleBioelectrocatalysis by redox enzymes at modified electrodes.


createdupdated
2004-07-092009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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