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EC Tree
IUBMB Comments The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
The enzyme appears in viruses and cellular organisms
Synonyms
glutathione peroxidase-like protein,
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glutathione peroxidase-like protein
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glutathione peroxidase-like protein-1
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glutathione peroxidase-like protein-2
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Gpx-1
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GPx-2
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a hydroperoxy fatty acid + NADPH + H+ = a hydroxy fatty acid + NADP+ + H2O
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hydroperoxy fatty acid:NADPH oxidorductase
The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
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alpha-linolenic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
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-
-
?
cumene hydroperoxide + NADPH + H+
? + NADP+ + H2O
-
-
-
?
linoleic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
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-
-
?
oleic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
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-
-
?
tert-butyl hydroperoxide + NADPH + H+
? + NADP+ + H2O
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-
-
?
additional information
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additional information
?
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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
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?
additional information
?
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the enzyme isoforms GPX-1 and GPX-2 do not utilize reduced glutathione and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides
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?
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NADPH
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-
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Ag+
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complete inhibition at 1 mM
Cu2+
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complete inhibition at 1 mM
N-ethylmaleimide
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60% inhibition of isoform Gpx-1 at 1 mM
p-chloromercuribenzoate
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30% inhibition of isoform Gpx-1 at 0.3 mM
additional information
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not inhibited by 1 mM cyanide and 1 mM azide
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0.0821 - 0.215
alpha-linolenic acid hydroperoxide
0.0821
alpha-linolenic acid hydroperoxide
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isoform Gpx-2, at pH 8.2 and 37°C
0.215
alpha-linolenic acid hydroperoxide
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isoform Gpx-1, at pH 8.2 and 37°C
0.0573
NADPH
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isoform Gpx-2, at pH 8.2 and 37°C
0.083
NADPH
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isoform Gpx-1, at pH 8.2 and 37°C
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0.8
Mercaptosuccinate
Synechocystis sp.
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isoform Gpx-1, at pH 8.2 and 37°C
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0.044
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isoform Gpx-1, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.053
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isoform Gpx-2, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.071
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isoform Gpx-1, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C
0.08
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isoform Gpx-2, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C
0.083
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isoform Gpx-1, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C
0.085
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isoform Gpx-2, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C
0.087
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isoform Gpx-1, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.106
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isoform Gpx-2, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.133
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isoform Gpx-1, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.15
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isoform Gpx-2, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C
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brenda
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physiological function
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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
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GPX2_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
154
0
16646
Swiss-Prot
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GPX1_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
169
0
18452
Swiss-Prot
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A0A5J4RVP2_9ZZZZ
185
1
21129
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A5J4PZ09_9ZZZZ
191
1
21548
TrEMBL
Secretory Pathway (Reliability: 2 )
A0A2H9T5Y2_9ZZZZ
171
0
19176
TrEMBL
other Location (Reliability: 2 )
A0A645EZ93_9ZZZZ
180
0
20340
TrEMBL
other Location (Reliability: 1 )
A0A645BY44_9ZZZZ
181
0
20609
TrEMBL
other Location (Reliability: 1 )
A0A5J4R9H3_9ZZZZ
100
1
11494
TrEMBL
Mitochondrion (Reliability: 4 )
A0A6I7D220_BACIU
160
0
18265
TrEMBL
-
A0A1V6EED8_9BACT
84
0
9105
TrEMBL
-
A0A1J5RI01_9ZZZZ
176
0
19348
TrEMBL
other Location (Reliability: 2 )
A0A3P5X140_9RHOB
168
0
18431
TrEMBL
-
A0A5P9J924_9RHOB
168
0
18431
TrEMBL
-
A0A1V6J7H9_9BACT
79
0
9342
TrEMBL
-
A0A644UYC0_9ZZZZ
162
0
18356
TrEMBL
other Location (Reliability: 2 )
A0A645IDA9_9ZZZZ
139
0
15022
TrEMBL
other Location (Reliability: 4 )
A0A644TT87_9ZZZZ
182
0
20543
TrEMBL
other Location (Reliability: 2 )
A0A645CVK9_9ZZZZ
178
0
19929
TrEMBL
other Location (Reliability: 1 )
A0A5J4Q0Y7_9ZZZZ
44
0
5103
TrEMBL
other Location (Reliability: 1 )
A0A1J5P578_9ZZZZ
166
0
19067
TrEMBL
other Location (Reliability: 1 )
A0A644WDA9_9ZZZZ
176
0
19913
TrEMBL
other Location (Reliability: 1 )
A0A6G9Q285_LACHI
157
0
17861
TrEMBL
-
A0A6G0ZVB2_9NEIS
159
0
17646
TrEMBL
-
A0A644YVZ0_9ZZZZ
181
0
20557
TrEMBL
other Location (Reliability: 1 )
A0A644Y1C7_9ZZZZ
181
0
20748
TrEMBL
other Location (Reliability: 2 )
A0A645DBB9_9ZZZZ
181
0
20762
TrEMBL
other Location (Reliability: 1 )
A0A5J4QJI3_9ZZZZ
183
0
20716
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A1J5T3D8_9ZZZZ
177
0
19804
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A6G9M1S6_9PSED
162
0
17620
TrEMBL
-
A0A5J4SXZ2_9ZZZZ
191
0
21586
TrEMBL
Secretory Pathway (Reliability: 2 )
A0A1J5RN60_9ZZZZ
187
0
20398
TrEMBL
Mitochondrion (Reliability: 4 )
A0A6H2HEE9_9BURK
205
0
22190
TrEMBL
-
A0A6H2H4M9_9BURK
162
0
17534
TrEMBL
-
A0A1V5L6K5_9PROT
91
0
10533
TrEMBL
-
A0A1J5SUF8_9ZZZZ
177
0
19945
TrEMBL
Secretory Pathway (Reliability: 2 )
A0A6G8NGX1_9BURK
159
0
17459
TrEMBL
-
A0A6G6E3C0_9BURK
159
0
17459
TrEMBL
-
A0A644Z9L2_9ZZZZ
159
0
18291
TrEMBL
other Location (Reliability: 1 )
A0A1J5QR49_9ZZZZ
199
0
21900
TrEMBL
Secretory Pathway (Reliability: 5 )
A0A644YXA1_9ZZZZ
159
0
18316
TrEMBL
other Location (Reliability: 1 )
A0A644VGL8_9ZZZZ
185
0
21029
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A644V0W3_9ZZZZ
184
1
20612
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A645JE20_9ZZZZ
82
0
8710
TrEMBL
other Location (Reliability: 3 )
A0A5J4QX50_9ZZZZ
200
1
22708
TrEMBL
Mitochondrion (Reliability: 3 )
A0A6G9M7G2_9PSED
161
0
17836
TrEMBL
-
A0A6I7BWC5_BACIU
160
0
18277
TrEMBL
-
A0A1J5PX88_9ZZZZ
75
0
8447
TrEMBL
other Location (Reliability: 2 )
A0A6G9M9C7_9PSED
184
0
20169
TrEMBL
-
A0A166H6Z2_9MICO
121
0
13420
TrEMBL
-
A0A6I7C9S6_BACIU
160
0
18261
TrEMBL
-
A0A5J4RCX0_9ZZZZ
185
1
21245
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A1J5PKR1_9ZZZZ
158
0
17478
TrEMBL
other Location (Reliability: 2 )
A0A315XMK4_9EURY
179
0
20496
TrEMBL
-
A0A1Q9NBW3_9ARCH
154
0
17637
TrEMBL
-
A0A2S9XXZ9_9DELT
102
0
11232
TrEMBL
-
A0A166C9M1_9EURY
179
0
20555
TrEMBL
-
A0A645ENX4_9ZZZZ
158
0
18028
TrEMBL
other Location (Reliability: 1 )
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16600
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isoform Gpx-2, gel filtration
16645
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1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence
18400
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isoform Gpx-1, gel filtration
18451
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1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence
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monomer
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1 * 16600, isoform Gpx-1, SDS-PAGE
monomer
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1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence
monomer
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1 * 18400, isoform Gpx-1, SDS-PAGE
monomer
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1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence
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ADP-Sepharose affinity column chromatography, gel filtration
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expressed in Escherichia coli BL21(DE3)pLysS cells
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no significant change in the protein level of GPX-2 is observed upon treatment with tert-butyl hydroperoxide
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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
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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
Plant Physiol.
136
2855-2861
2004
Synechocystis sp.
brenda
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
FEBS Lett.
499
32-36
2001
Synechocystis sp.
brenda
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1.11.1.22 hydroperoxy fatty acid reductase
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