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Information on EC 4.2.1.152 - hydroperoxy icosatetraenoate dehydratase and Organism(s) Homo sapiens and UniProt Accession Q9BYJ1
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4.2.1.152 hydroperoxy icosatetraenoate dehydrataseIUBMB Comments
Binds Fe2+. The mammalian enzymes accept a range of hydroperoxyicosatetraenoates (HPETE). The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency. The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE) . The enzymes also catalyse the reaction of EC 5.4.4.7, hydroperoxy icosatetraenoate isomerase.
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Word Map
- 4.2.1.152
- alox12b
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ichthyosiform
- erythroderma
-
lamellar
-
nipal4
-
abca12
- cyp4f22
- 12r-lox
- pnpla1
- harlequin
- 12r-lipoxygenase
- ichthyoses
-
hepoxilins
-
collodion
- lipoxygenase-3
-
sdr9c7
-
cornification
-
non-bullous
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galicia
-
self-healing
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corneocyte
-
self-improving
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, hepoxilin synthase, epidermis-type lipoxygenase 3, epidermal lox type 3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
hydroperoxyicosatetraenoate hydro-lyase (oxoicosatetraenoate-forming)
Binds Fe2+. The mammalian enzymes accept a range of hydroperoxyicosatetraenoates (HPETE). The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency. The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE) [2]. The enzymes also catalyse the reaction of EC 5.4.4.7, hydroperoxy icosatetraenoate isomerase.
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 + H2O
-
preferred substrate
-
-
?
(12R)-hydroperoxyeicosatetraenoic acid
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + 12-oxoeicosatetraenoic acid
-
preferred substrate
2:1 ratio, 2:1 product ratio
-
?
(12S)-hydroperoxyeicosatetraenoic acid
(10R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,8Z,14Z)-trienoic acid + (8R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + 12-oxoeicosatetraenoic acid
-
-
-
-
?
(15S)-hydroperoxyeicosatetraenoic acid
(13R)-hydroxy-(14S,15S)-epoxyeicosa-(5Z,8Z,11Z)-trienoic acid + 12-oxoeicosatetraenoic acid
-
-
-
-
?
(5S)-HPETE
(7R)-hydroxy-(5S,6S)-epoxyeicosa-(8Z,11Z,14Z)-trienoic acid + H2O
-
-
-
-
?
(5Z,8Z,10E,12R,14Z)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoate + H2O
-
-
-
-
?
(9E,11Z,14Z)-20:3omega6
(9S)-hydroperoxy-(10E,12E,14Z)-eicosatrienoic acid + H2O
-
good substrate
-
-
?
arachidonic acid + O2
5-HPETE + 7-HPETE + 9-HPETE
-
in the absence of fatty acid hydroperoxides, the enzyme shows only weak and slow activity with arachidonic acid
22%, 25%, and 29% yield, respectively
-
?
arachidonoyl-lysophosphatidic acid
15-HPETE-lysophosphatidic acid + 13-HPETE-lysophosphatidic acid + 11HPETE-lysophosphatidic acid + 5-HPETE-lysophosphatidic acid + H2O
-
-
36%, 22%, 21%, and 13% yield, respectively
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + H2O
-
preferred substrate
-
-
?
(12R)-hydroperoxyeicosatetraenoic acid
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + 12-oxoeicosatetraenoic acid
-
preferred substrate
2:1 ratio
-
?
(5S)-HPETE
(7R)-hydroxy-(5S,6S)-epoxyeicosa-(8Z,11Z,14Z)-trienoic acid + H2O
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nordihydroguaiaretic acid
-
submicromolar concentrations of nordihydroguaiaretic acid cause a dose-dependent increase in reaction rate 83-4fold with 12R-HPETE and up to 6fold with 15S-HPETE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression analysis of the enzyme in normal human skin and tissue-engineered skin substitutes, overview. Human TESS are models of epidermal differentiation expressing various epidermal markers. Normal human skin and TESS present the four expected epidermal layers: the basal, spinous, granular, and cornified layers. Enzyme eLOX3 is similarly expressed in TESS when compared with normal human skin
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the lipoxygenase (LOX) family contains enzymes catalyzing dioxygenation or, for epidermis-type lipoxygenase 3 (eLOX-3), hydroperoxide isomerization of polyunsaturated fatty acids. Five LOX mRNAs are known to be expressed in human epidermal cells: eLOX-3, 12R-lipoxygenase (12RLOX), 12S-lipoxygenase (12S-LOX), 15-lipoxygenase 1 (15-LOX-1), and 15-lipoxygenase 2 (15-LOX-2), expression profiles, overview
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)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A451G
-
unlike wild type enzyme, the mutant reacts well with arachidonic acid even in the absence of fatty acid hydroperoxides, yet only after an unusually long lag phase of about 20 min
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
Zheng, Y.; Brash, A.R.
Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids
J. Biol. Chem.
285
39866-39875
2010
Homo sapiens
Yu, Z.; Schneider, C.; Boeglin, W.E.; Brash, A.R.
Epidermal lipoxygenase products of the hepoxilin pathway selectively activate the nuclear receptor PPARalpha
Lipids
42
491-497
2007
Homo sapiens
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Release 2023.1 (January 2023)
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