PROSITE documentation PDOC00396 [for PROSITE entry PS00460]

Glutathione peroxidases signatures and profile





Description

Glutathione peroxidase (EC 1.11.1.9) (GSHPx) [1,2] is an enzyme that catalyzes the reduction of hydroxyperoxides by glutathione. Its main function is to protect against the damaging effect of endogenously formed hydroxyperoxides.

In higher vertebrates at least four forms of GSHPx are known to exist: a ubiquitous cytosolic form (GSHPx-1), a gastrointestinal cytosolic for (GSHPx-GI) [3], a plasma secreted form (GSHPx-P) [4], and a epididymal secretory form (GSHPx-EP). In addition to these characterized forms, the sequence of a protein of unknown function [5] has been shown to be evolutionary related to those of GSHPx's.

In filarial nematode parasites such as Brugia pahangi the major soluble cuticular protein, known as gp29, is a secreted GSHPx which could provide a mechanism of resistance to the immune reaction of the mammalian host by neutralizing the products of the oxidative burst of leukocytes [6].

Escherichia coli protein btuE, a periplasmic protein involved in the transport of vitamin B12, is also evolutionary related to GSHPx's; the significance of this relationship is not yet clear.

The catalyic site of GSHPx contains a conserved residue which is either a cysteine or, in many eukaryotic GSHPx, a selenocysteine [7]. The region around this active site residue can be used as a signature pattern. As a second signature for this family of proteins we selected a highly conserved octapeptide located in the central section of these proteins. We also developed a profile that covers the whole conserved region.

Last update:

January 2008 / Pattern updated.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

GLUTATHIONE_PEROXID_1, PS00460; Glutathione peroxidases active site  (PATTERN)

GLUTATHIONE_PEROXID_3, PS51355; Glutathione peroxidase profile  (MATRIX)

GLUTATHIONE_PEROXID_2, PS00763; Glutathione peroxidases signature 2  (PATTERN)


References

1AuthorsMannervik B.
TitleGlutathione peroxidase.
SourceMethods Enzymol. 113:490-495(1985).
PubMed ID4088069

2AuthorsMullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Tainer J.A., Hallewell R.A.
TitleSelenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases.
SourceProtein Eng. 2:239-246(1988).
PubMed ID2976939

3AuthorsChu F.F., Doroshow J.H., Esworthy R.S.
TitleExpression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI.
SourceJ. Biol. Chem. 268:2571-2576(1993).
PubMed ID8428933

4AuthorsTakahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J.
TitlePrimary structure of human plasma glutathione peroxidase deduced from cDNA sequences.
SourceJ. Biochem. 108:145-148(1990).
PubMed ID2229017

5AuthorsDunn D.K., Howells D.D., Richardson J.P., Goldfarb P.S.
TitleA human cDNA sequence for a novel glutathione peroxidase-related selenopeptide, GPRP.
SourceNucleic Acids Res. 17:6390-6390(1989).
PubMed ID2771650

6AuthorsCookson E., Blaxter M.L., Selkirk M.E.
TitleIdentification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase.
SourceProc. Natl. Acad. Sci. U.S.A. 89:5837-5841(1992).
PubMed ID1631065

7AuthorsStadtman T.C.
TitleSelenium biochemistry.
SourceAnnu. Rev. Biochem. 59:111-127(1990).
PubMed ID2142875
DOI10.1146/annurev.bi.59.070190.000551



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