Information on EC 1.11.1.22 - hydroperoxy fatty acid reductase

Word Map on EC 1.11.1.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Synechocystis sp.

EC NUMBER
COMMENTARY hide
1.11.1.22
-
RECOMMENDED NAME
GeneOntology No.
hydroperoxy fatty acid reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a hydroperoxy fatty acid + NADPH + H+ = a hydroxy fatty acid + NADP+ + H2O
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
cumene hydroperoxide + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
linoleic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
oleic acid hydroperoxide + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
tert-butyl hydroperoxide + NADPH + H+
? + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
complete inhibition at 1 mM
Cu2+
-
complete inhibition at 1 mM
Mercaptosuccinate
-
-
N-ethylmaleimide
-
60% inhibition of isoform Gpx-1 at 1 mM
p-chloromercuribenzoate
-
30% inhibition of isoform Gpx-1 at 0.3 mM
additional information
-
not inhibited by 1 mM cyanide and 1 mM azide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0821 - 0.215
alpha-linolenic acid hydroperoxide
0.0573 - 0.083
NADPH
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
Mercaptosuccinate
Synechocystis sp.
-
isoform Gpx-1, at pH 8.2 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.044
-
isoform Gpx-1, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.053
-
isoform Gpx-2, using oleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.071
-
isoform Gpx-1, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C
0.08
-
isoform Gpx-2, using cumene hydroperoxide as substrate, at pH 8.2 and 37°C
0.083
-
isoform Gpx-1, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C
0.085
-
isoform Gpx-2, using tert-butyl hydroperoxide as substrate, at pH 8.2 and 37°C
0.087
-
isoform Gpx-1, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.106
-
isoform Gpx-2, using alpha-linoleic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.133
-
isoform Gpx-1, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C
0.15
-
isoform Gpx-2, using alpha-linolenic acid hydroperoxide as substrate, at pH 8.2 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16600
-
isoform Gpx-2, gel filtration
16645
-
1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence
18400
-
isoform Gpx-1, gel filtration
18451
-
1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 16600, isoform Gpx-1, SDS-PAGE; 1 * 16645, isoform Gpx-2, calculated from deduced amino acid sequence; 1 * 18400, isoform Gpx-1, SDS-PAGE; 1 * 18451, isoform Gpx-1, calculated from deduced amino acid sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-Sepharose affinity column chromatography, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no significant change in the protein level of GPX-2 is observed upon treatment with tert-butyl hydroperoxide
-
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
-