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Literature summary for 1.11.1.22 extracted from

  • Gaber, A.; Yoshimura, K.; Tamoi, M.; Takeda, T.; Nakano, Y.; Shigeoka, S.
    Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress (2004), Plant Physiol., 136, 2855-2861.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme isoforms GPX-1 and GPX-2 do not utilize reduced glutathione and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides Synechocystis sp. ?
-
 ?
tert-butyl hydroperoxide + NADPH + H+
-
 Synechocystis sp. ? + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
glutathione peroxidase-like protein
-
 Synechocystis sp.
Gpx-1 isoform Synechocystis sp.
GPx-2 isoform Synechocystis sp.
slr1171
-
 Synechocystis sp.
slr1992
-
 Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Synechocystis sp.

Expression

Organism Comment Expression
Synechocystis sp. no significant change in the protein level of GPX-2 is observed upon treatment with tert-butyl hydroperoxide additional information
Synechocystis sp. the steady-state transcript level of gpx-1 gradually increases under oxidative stress conditions imposed by high light intensity (0.35 mE m.2 s-1), high salinity (200 mM NaCl), or application of methyl viologen (0.001 mM) or tert-butyl hydroperoxide (0.001 mM) in the wild type and GPX-2 knock-out mutant cells. The protein level of GPX-2 increases approximately 3fold and 1.6fold at 3 h with the methyl viologen and NaCl treatments, respectively. Under high light conditions, the protein level of GPX-2 increases approximately 1.2fold up

General Information

General Information Comment Organism
physiological function isoforms GPX-1 and GPX-2 are essential for the removal of lipid hydroperoxides under normal and stress conditions, leading to the protection of membrane integrity Synechocystis sp.