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Information on EC 5.4.4.7 - hydroperoxy icosatetraenoate isomerase and Organism(s) Mus musculus and UniProt Accession Q9WV07

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.4 Transferring hydroxy groups
                5.4.4.7 hydroperoxy icosatetraenoate isomerase
IUBMB Comments
Binds Fe2+. The enzyme from mammals accepts a range of hydroperoxyicosatetraenoates producing one or several different hydroxyepoxyicosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate . The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate . The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase.
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Mus musculus
UNIPROT: Q9WV07
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ALOXE3, eLOX-3, eLOX3, epidermal lipoxygenase-3, epidermal LOX type 3, hepoxilin synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epidermal lipoxygenase-3
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eLOX3
-
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epidermal lipoxygenase-3
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
hydroperoxyicosatetraenoate hydroxymutase
Binds Fe2+. The enzyme from mammals accepts a range of hydroperoxyicosatetraenoates producing one or several different hydroxyepoxyicosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate [1]. The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate [2]. The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(12R)-HPETE
?
show the reaction diagram
-
-
-
-
?
(5S)-HPETE
(7R)-hydroxy-(5S,6S)-epoxyeicosa-(8Z,11Z,14Z)-trienoic acid
show the reaction diagram
-
-
-
-
?
(8R)-HPETE
8-KETE
show the reaction diagram
-
best substrate
-
-
?
(8S)-HPETE
(10R)-hydroxy-(8S,9S)-epoxyeicosa-(5Z,11Z,14Z)-trienoic acid
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
intra-amniotic delivery of epidermal lipoxygenase-3 (eLOX-3) to mice at gestational day 14.5, both via an adenoviral vector and as recombinant protein, results in fetal growth restriction and intrauterine death. Periodic acid-Schiff staining and RT-PCR analysis of placentae from fetuses exposed to eLOX-3 indicate a lack of glycogen trophoblasts in the junctional zone. Placenta-specific gene expression is altered. Thus, the observed prenatal toxicity of eLOX-3 can be due to a strong effect on placental development. Placentae from eLOX-3-exposed fetuses have an altered structure. Short life-span of eLOX-3 null mice
physiological function
metabolites of the epidermal lipoxygenase-3 (eLOX-3) are involved in various metabolic pathways. Intra-amniotic delivery of eLOX-3 to mice at gestational day 14.5, both via an adenoviral vector and as recombinant protein, results in fetal growth restriction and intrauterine death. Periodic acid-Schiff staining and RT-PCR analysis of placentae from fetuses exposed to eLOX-3 indicate a lack of glycogen trophoblasts in the junctional zone. Placenta-specific gene expression is altered. Thus, the observed prenatal toxicity of eLOX-3 can be due to a strong effect on placental development. eLOX-3 appears to have some impact on the expression of genes that indirectly influence fetal development
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOXE3_MOUSE
711
0
80473
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
intra-amniotic delivery of eLOX-3 to mice at gestational day 14.5, both via an adenoviral vector and as recombinant protein, expression of the placenta-specific genes Tpbpa, Pcdh12, Muc1, Gcm1, SynA, and PL-1, encoding trophoblast-specific protein alpha, protocadherin 12, mucin 1, glial cell missing homologue 1, syncytin A, and placental lactogen 1, respectively, is analyzed in SYBR green-based real-time RT-PCR assays. Analysis of toxicity of eLOX-3 and dose-dependence of fetal survival, overview. Placentae from eLOX-3-exposed fetuses have an altered structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Aloxe3, intra-amniotic delivery of eLOX-3 to mice at gestational day 14.5, both via an adenoviral vector and as recombinant protein
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, Z.; Schneider, C.; Boeglin, W.E.; Brash, A.R.
Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin
Arch. Biochem. Biophys.
455
188-196
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Vierling, F.; Dick, A.; Wahlbuhl, M.; Krieg, P.; Henke, C.; Ruebner, M.; Schneider, H.
Surprising prenatal toxicity of epidermal lipoxygenase-3
Placenta
35
776-779
2014
Mus musculus (Q9WV07)
Manually annotated by BRENDA team