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Information on EC 5.4.4.7 - hydroperoxy icosatetraenoate isomerase and Organism(s) Homo sapiens
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5.4.4.7 hydroperoxy icosatetraenoate isomeraseIUBMB 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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Word Map
- 5.4.4.7
- alox12b
-
ichthyosiform
-
lamellar
- erythroderma
-
cyp4f22
-
abca12
-
nipal4
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pnpla1
- harlequin
- 12r-lox
-
collodion
- lipoxygenase-3
- 12r-lipoxygenase
-
non-bullous
-
cornification
- ichthyoses
-
epidermis-type
-
hyperkeratosis
-
self-healing
-
galicia
-
hepoxilins
-
epoxyalcohol
-
corneocyte
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ALOXE3, eLOX-3, eLOX3, epidermal lipoxygenase-3, epidermal LOX type 3, hepoxilin synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(12R)-HPETE
(8R)-hydroxy-(11R,12R)- epoxyeicosa-(5Z,9E,14Z)-trienoic acid
-
preferred substrate
-
-
?
(12R)-HPETE
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid
-
-
-
-
?
(12R)-HPETE
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + 12-oxoeicosatetraenoic acid
-
preferred substrate
2:1 ratio
-
?
(12S)-HPETE
(10R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,8Z,14Z)-trienoic acid + (8R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid
-
-
-
-
?
(15S)-HPETE
(13R)-hydroxy-(14S,15S)-epoxyeicosa-(5Z,8Z,11Z)-trienoic acid
-
-
-
-
?
(5S)-HPETE
(7R)-hydroxy-(5S,6S)-epoxyeicosa-(8Z,11Z,14Z)-trienoic acid
-
-
-
-
?
(8S)-HPETE
(10R)-hydroxy-(8S,9S)-epoxyeicosa-(5Z,11Z,14Z)-trienoic acid
-
-
-
-
?
additional information
?
-
-
linoleic, arachidonic, and eicosapentaenoic acids, the methyl esters of arachidonic acid and linoleic acid, arachidonyl phosphatidylcholine, anandamide, and the cholesteryl ester of arachidonic acid are no substrates
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
eLOX3, is not a functional lipoxygenase enzyme, but has catalytic activity as a hydroperoxide isomerase
physiological function
-
the enzyme participates in the normal process of skin differentiation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LOXE3_HUMAN
711
0
80543
Swiss-Prot
other Location (Reliability: 4)
CP2J2_HUMAN
502
2
57611
Swiss-Prot
Secretory Pathway (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, Z.; Schneider, C.; Boeglin, W.E.; Marnett, L.J.; Brash, A.R.
The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase
Proc. Natl. Acad. Sci. USA
100
9162-9167
2003
Homo sapiens
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
Yu, Z.; Schneider, C.; Boeglin, W.E.; Brash, A.R.
Mutations associated with a congenital form of ichthyosis (NCIE) inactivate the epidermal lipoxygenases 12R-LOX and eLOX3
Biochim. Biophys. Acta
1686
238-247
2005
Homo sapiens
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