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Information on EC 1.13.11.31 - arachidonate 12-lipoxygenase and Organism(s) Danio rerio

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EC Tree
IUBMB Comments
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
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This record set is specific for:
Danio rerio
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
12-lipoxygenase, 15-lipoxygenase, 12-lox, alox5, 15-lox-1, alox15, 12-lo, 15-lo, 12/15-lipoxygenase, 12/15-lox, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12-lipoxygenase
12-LOX
12/15-lipoxygenase
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-
-
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12DELTA-lipoxygenase
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-
-
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12S-lipoxygenase
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-
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C-12 lipoxygenase
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-
-
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DELTA 12-lipoxygenase
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leukotriene A4 synthase M
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-
-
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LTA4 synthase
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-
-
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oygenase, arachidonate 12-lip-
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-
-
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Platelet-type lipoxygenase 12
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydration
-
-
-
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dioxygenation
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-
-
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oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 12-oxidoreductase
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
CAS REGISTRY NUMBER
COMMENTARY hide
82391-43-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the specific activity of recombinant soluble zf12-LOX mutant is increased by nearly 75% (25 nmol/min/mg) in the presence of calcium as compared to that in its absence (7 nmol/min/mg), while for the site-2 mutant, it is 5 nmol/min/mg irrespective of the presence of calcium. Ca2+ decreases the aggregation temperature of soluble zf12-LOX mutant, while secondary structure is maintained. Presence of Ca2+ induces increase in molecular dimensions of soluble zf12-LOX mutant
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is required for normal embryonic development in the fish
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8M1P9T6_DANRE
670
0
77007
TrEMBL
other Location (Reliability: 1)
Q7T2A9_DANRE
670
0
77007
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 75000, recombinant His-tagged enzyme, SDS-PAGE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on Ni column
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligated into the pQE-9 plasmid and expressed as N-terminal His-tag fusion protein in Escherichia coli (XL-1 Blue)
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recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walther, M.; Roffeis, J.; Jansen, C.; Anton, M.; Ivanov, I.; Kuhn, H.
Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms
Biochim. Biophys. Acta
1791
827-835
2009
Danio rerio, Mus musculus
Manually annotated by BRENDA team
Mittal, M.; Hasan, M.; Balagunaseelan, N.; Fauland, A.; Wheelock, C.; Radmark, O.; Haeggstroem, J.; Rinaldo-Matthis, A.
Investigation of calcium-dependent activity and conformational dynamics of zebra fish 12-lipoxygenase
Biochim. Biophys. Acta
1861
2099-2111
2017
Danio rerio (Q7T2A9), Danio rerio
Manually annotated by BRENDA team