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Literature summary for 1.11.1.22 extracted from

  • Gaber, A.; Tamoi, M.; Takeda, T.; Nakano, Y.; Shigeoka, S.
    NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803 (2001), FEBS Lett., 499, 32-36.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3)pLysS cells Synechocystis sp.

Inhibitors

Inhibitors Comment Organism Structure
Ag+ complete inhibition at 1 mM Synechocystis sp.
Cu2+ complete inhibition at 1 mM Synechocystis sp.
Mercaptosuccinate
-
Synechocystis sp.
additional information not inhibited by 1 mM cyanide and 1 mM azide Synechocystis sp.
N-ethylmaleimide 60% inhibition of isoform Gpx-1 at 1 mM Synechocystis sp.
p-chloromercuribenzoate 30% inhibition of isoform Gpx-1 at 0.3 mM Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0573
-
NADPH isoform Gpx-2, at pH 8.2 and 37°C Synechocystis sp.
0.0821
-
alpha-linolenic acid hydroperoxide isoform Gpx-2, at pH 8.2 and 37°C Synechocystis sp.
0.083
-
NADPH isoform Gpx-1, at pH 8.2 and 37°C Synechocystis sp.
0.215
-
alpha-linolenic acid hydroperoxide isoform Gpx-1, at pH 8.2 and 37°C Synechocystis sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16600
-
isoform Gpx-2, gel filtration Synechocystis sp.
16645
-
1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence Synechocystis sp.
18400
-
isoform Gpx-1, gel filtration Synechocystis sp.
18451
-
1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ADP-Sepharose affinity column chromatography, gel filtration Synechocystis sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.044
-
isoform Gpx-1, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.053
-
isoform Gpx-2, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.071
-
isoform Gpx-1, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.08
-
isoform Gpx-2, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.083
-
isoform Gpx-1, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.085
-
isoform Gpx-2, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.087
-
isoform Gpx-1, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.106
-
isoform Gpx-2, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.133
-
isoform Gpx-1, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.
0.15
-
isoform Gpx-2, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-linolenic acid hydroperoxide + NADPH + H+
-
Synechocystis sp. ? + NADP+ + H2O
-
?
cumene hydroperoxide + NADPH + H+
-
Synechocystis sp. ? + NADP+ + H2O
-
?
linoleic acid hydroperoxide + NADPH + H+
-
Synechocystis sp. ? + NADP+ + H2O
-
?
additional information the enzyme does not use reduced glutathione as an electron donor. No activity with H2O2, phosphatidylcholine hydroperoxide and digalactosyl diacylglycerol hydroperoxide. Neither cytochrome c nor ascorbate substitute for NADPH as an electron donor Synechocystis sp. ?
-
?
oleic acid hydroperoxide + NADPH + H+
-
Synechocystis sp. oleic acid + NADP+ + H2O
-
?
tert-butyl hydroperoxide + NADPH + H+
-
Synechocystis sp. ? + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
monomer 1 * 16600, isoform Gpx-1, SDS-PAGE Synechocystis sp.
monomer 1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence Synechocystis sp.
monomer 1 * 18400, isoform Gpx-1, SDS-PAGE Synechocystis sp.
monomer 1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence Synechocystis sp.

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
NADPH dependent on Synechocystis sp.

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.8
-
isoform Gpx-1, at pH 8.2 and 37°C Synechocystis sp. Mercaptosuccinate