Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.13.11.31 - arachidonate 12-lipoxygenase and Organism(s) Sus scrofa and UniProt Accession P16469

for references in articles please use BRENDA:EC1.13.11.31
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The product is rapidly reduced to the corresponding 12S-hydroxy compound.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
UNIPROT: P16469
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Sus scrofa
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
-
leukocyte-type 12-lipoxygenase
-
leukocyte-type 12-LOX
-
12-lipoxygenase
12-LOX
-
-
-
-
12/15-lipoxygenase
12/15-LO
-
-
12/15LO
-
-
12DELTA-lipoxygenase
-
-
-
-
12S-lipoxygenase
-
-
-
-
C-12 lipoxygenase
-
-
-
-
DELTA 12-lipoxygenase
-
-
-
-
leukotriene A4 synthase M
-
-
-
-
LTA4 synthase
-
-
-
-
oygenase, arachidonate 12-lip-
-
-
-
-
Platelet-type lipoxygenase 12
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
dioxygenation
-
-
-
-
dehydration
-
-
-
-
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
-
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
-
-
-
?
arachidonic acid + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
?
(Z,Z,Z,E)-5,8,11,13-eicosatetraenoic acid + O2
?
show the reaction diagram
-
-
-
-
?
1-linoleoyl lysophosphatidic acid + O2
(S)-hydroperoxy 1-linoleoyl lysophosphatidic acid
show the reaction diagram
-
i.e. linoleoyl-lysoPA
major product
-
?
1-linoleoyl lysophosphatidylcholine + O2
(S)-hydroperoxy 1-linoleoyl lysophosphatidylcholine
show the reaction diagram
-
i.e. linoleoyl-lysoPC
major product
-
?
11,14,17-eicosatrienoic acid + O2
?
show the reaction diagram
-
enzyme from leukocyte
-
-
?
11,14-eicosadienoic acid + O2
?
show the reaction diagram
-
enzyme from leukocyte
-
-
?
4,7,10,13,16,19-docosahexaenoic acid + O2
?
show the reaction diagram
-
-
-
-
?
5(S)-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid + O2
5,12-(5S,12S)-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5,12-(5S,15S)-dihydroxy-6E,8Z,11Z,13E-eicosatetraenoic acid
show the reaction diagram
5,15-(5S,15S)-dihydroperoxyarachidonic acid + O2
5S,14R,15S-trihydroperoxy-6,10,12-trans-8-cis-eicosatetraenoic acid
show the reaction diagram
-
-
the product is reduced to 5S,14R,15S,-8-cis-lipoxin B due to 14R-oxygenase activity of the enzyme
?
5,8,11,14,17-eicosapentaenoic acid + O2
12-hydroxy-5,8,10,14,17-eicosapentaenoic acid
show the reaction diagram
8,11,14-eicosatrienoic acid + O2
12-hydroxyeicosatrienoic acid
show the reaction diagram
alpha-linolenic acid + O2
?
show the reaction diagram
-
activity with enzyme from leukocyte
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
show the reaction diagram
gamma-linolenic acid + O2
10-hydroxy-octadeca-6Z,8E,12Z-trienoic acid
show the reaction diagram
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleic acid + O2
13(S)-hydroperoxy-9Z,11E-octadecadienoic acid
show the reaction diagram
15(S)-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid + O2
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
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
pathway of lipoxin biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
0.94 atoms of iron per molecule. Loss of the mass of an iron atom from the protein as the pH is lowered from 5 to 4. The iron goes through acid-induced unfolding accompanied by the appearance of an iron-free intermediate that retains a native conformation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octa-dienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-cis-p-coumaroyl)-beta-D-glucopyranoside
liguroside B, NMR spectral analysis
(2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octadienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-trans-p-coumaroyl)-beta-D-glucopyranoside
liguroside A, NMR spectral analysis
4-(2-oxapentadeca-4-yne) phenylpropanoic acid
-
epigallocatechin gallate
-
kudingoside B
NMR spectral analysis
2,2'-dipyridyl
-
1 mM, 87% inactivation, no reactivation by addition of excess Fe2+ or Fe3+
4-(2-oxapentadeca-4-yne)phenylpropanoic acid
5,8,11,14-Eicosatetraynoic acid
arachidonic acid
BW755C
-
0.01 mM, 72% inhibition
BWA137C
-
-
N-(4-chlorophenyl)-N-hydroxy-N'-(3-chlorophenyl)urea
-
-
nordihydroguaiaretic acid
additional information
Chinese tea Qing Shan Lu Shui, which contains lower catechin levels than the other tested teas, inhibits the enzyme activity, 12-LOX inhibitory activity–guided fractionation of the aqueous ethanol extract are used to isolate twp components: monoterpene glycosides liguroside A and liguroside B, i.e. (2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octadienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-trans-p-coumaroyl)-beta-D-glucopyranoside and (2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octa-dienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-cis-p-coumaroyl)-beta-D-glucopyranoside, respectively. Inhibitory effect on leukocyte-type 12-LOX activity and catechin contents of 12 Chinese teas, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0039
(Z,Z,Z,E)-5,8,11,13-eicosatetraenoic acid
-
-
0.0355
1-linoleoyl lysophosphatidic acid
-
pH 7.5, 25°C
0.0151
1-linoleoyl lysophosphatidylcholine
-
pH 7.5, 25°C
0.0045
5(S)-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid
-
-
0.004 - 0.022
arachidonic acid
0.03 - 0.0312
linoleic acid
additional information
additional information
-
kinetics with lysophospholipid substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.2 - 18
arachidonic acid
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.07
4-(2-oxapentadeca-4-yne)phenylpropanoic acid
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007
(2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octa-dienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-cis-p-coumaroyl)-beta-D-glucopyranoside
Sus scrofa
pH 7.4, 30°C, recombinant leukocyte-type enzyme
0.0017
(2E,5E)-7-hydroperoxy-3,7-dimethyl-2,5-octadienyl-O-(alpha-L-rhamnopyranosyl)-(1''->3')-(4'''-O-trans-p-coumaroyl)-beta-D-glucopyranoside
Sus scrofa
pH 7.4, 30°C, recombinant leukocyte-type enzyme
0.00006
5,8,11,14-Eicosatetraynoic acid
Sus scrofa
-
IC50: 0.00006 mM
0.0022
nordihydroguaiaretic acid
Sus scrofa
-
IC50: 0.0022 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
purified enzyme
0.033
-
-
1.7
-
-
51.8
-
commercial preparation
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
30
assay at
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
-
Plox-86 cells overexpress leukocyte-type 12/15-LO. Significant increase of monocyte chemoattractant protein-1 mRNA in Plox-86 cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX15_PIG
663
0
75004
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74700
1 * 74700, dynamic light scattering
72000
-
x * 72000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 74700, dynamic light scattering
?
-
x * 72000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals diffracting to high resolution (1.9 A) are obtained for a complex between the catalytic domain of leukocyte 12-lipoxygenase and the isoform-specific inhibitor, 4-(2-oxapentadeca-4-yne) phenylpropanoic acid (OPP)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M338L
-
Km-value for arachidonic acid is about 1/2 that of the wild type enzyme
M367V
-
Km-value for arachidonic acid and turnover number are approximately double that of the wild-type enzyme
M562L
-
Km-value for arachidonic acid is 77% of that of the wild type enzyme, turnover number is 85% of that of the wild type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
half-life: 24 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
15-25% loss of activity upon freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 1 month
-
-70°C, 20% glycerol, 10 mM 2-mercaptoethanol, 0.3% Triton X-305, enzyme retains complete activity after 1 month
-
-80°C, stable for at least 4 months
-
4°C, half-life: 24 h, markedly stabilized by 0.02 mM Fe2+
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion exchange chromatography
recombinant enzyme partiallay from J774A.1 cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed from pET-20b(+) plasmid in Escherichia coli Rosetta 2 (DE3) cells
expressed in Escherichia coli
recombinant overexpression in J774A.1 cells
12/15LO stably overexpressed in mouse J774 macrophages
-
enzyme is cloned into the expression vectors pSE280, pSE380, and pSE420. PSE380 yields the highest level of 12-lipoxygenase activity, expression in Escherichia coli Top10 cells
-
expression in insect cells using a baculovirus expression vector, expression as an N-terminal fusion protein with a 31-amino acid polypeptide carrying a six-histidine tag and an enterokinase cleavage site
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuda, S.; Suzuki, H.; Yoshimoto, T.; Yamamoto, S.; Miyatake, A.
Analysis of non-heme iron in arachidonate 12-lipoxygenase of porcine leukocytes
Biochim. Biophys. Acta
1084
202-204
1991
Sus scrofa
Manually annotated by BRENDA team
Hada, T.; Ueda, N.; Takahashi, Y.; Yamamoto, S.
Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins
Biochim. Biophys. Acta
1083
89-93
1991
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Kroneck, P.M.H.; Cucurou, C.; Ullrich, V.; Ueda, N.; Suzuki, H.; Yoshimoto, T.; Matsuda, S.; Yamamoto, S.
Porcine leukocyte 5- and 12-lipoxygenases are iron enzymes
FEBS Lett.
287
105-107
1991
Sus scrofa
Manually annotated by BRENDA team
Labelle, M.; Falgueyret, J.P.; Riendeau, D.; Rokach, J.
Synthesis of two analogues of arachidonic acid and their reactions with 12-lipoxygenase
Tetrahedron
46
6301-6310
1990
Sus scrofa
-
Manually annotated by BRENDA team
Brash, A.R.; Yokoyama, C.; Oates, J.A.; Yamamoto, S.
Mechanistic studies of the dioxygenase and leukotriene synthase activities of the porcine leukocyte 12S-lipoxygenase
Arch. Biochem. Biophys.
273
414-422
1989
Sus scrofa
Manually annotated by BRENDA team
Yokoyama, C.; Shinjo, F.; Yoshimoto, T.; Yamamoto, S.; Oates, J.A.; Brash, A.R.
Arachidonate 12-lipoxygenase purified from porcine leukocytes by immunoaffinity chromatography and its reactivity with hydroperoxyeicosatetraenoic acids
J. Biol. Chem.
261
16714-16721
1986
Sus scrofa
Manually annotated by BRENDA team
Ueda, N.; Yokoyama, C.; Yamamoto, S.; Fitzsimmons, B.J.; Rokach, J.; Oates, J.A.; Brash, A.R.
Lipoxin synthesis by arachidonate 12-lipoxygenase purified from porcine leukocytes
Biochem. Biophys. Res. Commun.
149
1063-1069
1987
Sus scrofa
Manually annotated by BRENDA team
Shinjo, F.; Yoshimoto, T.; Yokoyama, C.; Yamamoto, S.; Izumi, S.I.; Komatsu, N.; Watanabe, K.
Studies on porcine arachidonate 12-lipoxygenase using its monoclonal antibodies
J. Biol. Chem.
261
3377-3381
1986
Sus scrofa
Manually annotated by BRENDA team
Yoshimoto, T.; Miyamoto, Y.; Ochi, K.; Yamamoto, S.
Arachidonate 12-lipoxygenase of porcine leukocyte with activity for 5-hydroxyeicosatetraenoic acid
Biochim. Biophys. Acta
713
638-646
1982
Sus scrofa
Manually annotated by BRENDA team
Richards, K.M.; Marnett, L.J.
Leukocyte 12-lipoxygenase: Expression, purification, and investigation of the role of methionine residues in turnover-dependent inactivation and 5,8,11,14-eicosatetraynoic acid inhibition
Biochemistry
36
6692-6699
1997
Sus scrofa
Manually annotated by BRENDA team
Reddy, R.G.; Yoshimoto, T.; Yamamoto, S.; Funk, C.D.; Marnett, L.J.
Expression of porcine leukocyte 12-lipoxygenase in a baculovirus/insect cell system and its characterization
Arch. Biochem. Biophys.
312
219-226
1994
Sus scrofa
Manually annotated by BRENDA team
Moody, J.S.; Marnett, L.J.
Kinetics of Inhibition of Leukocyte 12-Lipoxygenase by the Isoform-Specific Inhibitor 4-(2-Oxapentadeca-4-yne)phenylpropanoic Acid
Biochemistry
41
10297-10303
2002
Sus scrofa
Manually annotated by BRENDA team
Richards, K.M.; Moody, J.S.; Marnett, L.J.
Mechanism of Inhibition of Porcine Leukocyte 12-Lipoxygenase by the Isoform-Specific Inhibitor 4-(2-Oxapentadeca-4-yne)phenylpropanoic Acid
Biochemistry
38
16529-16538
1999
Sus scrofa
Manually annotated by BRENDA team
Wen, Y.; Gu, J.; Vandenhoff, G.E.; Liu, X.; Nadler, J.L.
Role of 12/15-lipoxygenase in the expression of MCP-1 in mouse macrophages
Am. J. Physiol. Heart Circ. Physiol.
294
H1933-H1938
2008
Mus musculus, Sus scrofa
Manually annotated by BRENDA team
Huang, L.S.; Kim, M.R.; Jeong, T.S.; Sok, D.E.
Linoleoyl lysophosphatidic acid and linoleoyl lysophosphatidylcholine are efficient substrates for mammalian lipoxygenases
Biochim. Biophys. Acta
1770
1062-1070
2007
Sus scrofa
Manually annotated by BRENDA team
Rapp, J.; Xu, S.; Sharp, A.M.; Griffith, W.P.; Kim, Y.W.; Funk, M.O.
EPR spectroscopy and electrospray ionization mass spectrometry reveal distinctive features of the iron site in leukocyte 12-lipoxygenase
Arch. Biochem. Biophys.
490
50-56
2009
Sus scrofa (P16469), Sus scrofa
Manually annotated by BRENDA team
Nagelin, M.H.; Srinivasan, S.; Lee, J.; Nadler, J.L.; Hedrick, C.C.
12/15-Lipoxygenase activity increases the degradation of macrophage ATP-binding cassette transporter G1
Arterioscler. Thromb. Vasc. Biol.
28
1811-1819
2008
Sus scrofa
Manually annotated by BRENDA team
Xu, S.; Mueser, T.C.; Marnett, L.J.; Funk, M.O.
Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis
Structure
20
1490-1497
2012
Sus scrofa (P16469)
Manually annotated by BRENDA team
Ito, H.; Otsuki, A.; Mori, H.; Li, P.; Kinoshita, M.; Kawakami, Y.; Tsuji, H.; Fang, D.; Takahashi, Y.
Two new monoterpene glycosides from Qing Shan Lu Shui tea with inhibitory effects on leukocyte-type 12-lipoxygenase activity
Molecules
18
4257-4266
2013
Sus scrofa (P16469)
Manually annotated by BRENDA team