Entry |
|
Name |
hydroperoxy icosatetraenoate dehydratase;
epidermal lipoxygenase-3 (ambiguous);
eLOX3 (ambiguous)
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Class |
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
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Sysname |
hydroperoxyicosatetraenoate hydro-lyase (oxoicosatetraenoate-forming)
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Reaction(IUBMB) |
a hydroperoxyicosatetraenoate = an oxoicosatetraenoate + H2O [RN: R10761]
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Reaction(KEGG) |
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Substrate |
hydroperoxyicosatetraenoate [CPD: C20832]
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Product |
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Comment |
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.
|
History |
EC 4.2.1.152 created 2014
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Orthology |
K18684 | hydroperoxy icosatetraenoate dehydratase/isomerase |
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Genes |
» show all
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Reference |
|
Authors |
Yu Z, Schneider C, Boeglin WE, Marnett LJ, Brash AR |
Title |
The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase. |
Journal |
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Sequence |
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Reference |
|
Authors |
Yu Z, Schneider C, Boeglin WE, Brash AR |
Title |
Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin. |
Journal |
|
Sequence |
|
Reference |
|
Authors |
Zheng Y, Brash AR |
Title |
Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids. |
Journal |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 4.2.1.152 |
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