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(15S)-hydroperoxyeicosatetraenoic acid + O2
?
-
-
-
-
?
(15S)-hydroxyeicosatetraenoic acid + O2
?
-
-
-
-
?
(5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid + O2
?
-
8-LOX tolerates a carboxylic group in the substrate-binding pocket
-
-
?
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid + O2
(8S,15S)-dihydroperoxy-5Z,9E,11Z,13E-eicosatetraenoic acid
-
-
-
-
?
(8S)-hydroxyeicosatetraenoic acid + O2
?
-
-
-
-
?
17S-hydroxy-docosa-4Z,7Z,10Z,13Z,15E,19Z-hexaenoic acid + O2
10R,17S-dihydroxy-docosa-4Z,7Z,11E,13Z,15E,19Z-hexaenoic acid
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
5-hydroperoxy fatty acid + O2
leukotriene A4
-
leukotriene A synthase activity, reaction rate is approximately 7% of arachidonate 8-lipoxygenation
-
-
?
5-hydroperoxyeicosatetraenoic acid + ?
leukotriene A4
-
-
unstable product
?
alpha-linolenic acid + O2
?
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
arachidonate + O2
(5Z,9E,11Z,14Z)-(8S)-8-hydroperoxyeicosa-5,9,11,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8S)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(5Z,8E,11Z,14Z)-8-hydroperoxyicosa-5,8,11,14-tetraenoic acid + (5Z,8E,11Z,14Z)-8-hydroxyicosa-5,8,11,14-tetraenoic acid
-
arachidonic acid, enzyme activity only detectable after in vivo treatment with the phorbol ester tumor promoter TPA (12-O-tetradecanoylphorbol-13-acetate)
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
arachidonic acid + O2
8R-hydroxy-eicosatetraenoic acid
-
-
-
?
docosahexaenoic acid + O2
10R-hydroxy-docosahexaenoic acid
-
-
-
?
docosahexaenoic acid + O2
?
-
-
-
-
?
eicosapentaenoic acid + O2
8R-hydroxy-eicosapentaenoic acid
-
-
-
?
eicosapentaenoic acid + O2
?
-
-
-
-
?
gamma-linoleic acid + O2
?
-
-
-
-
?
linoleic acid + O2
?
-
poor substrate
-
-
?
stearidonic acid + O2
6-hydroxystearidonic acid
-
-
-
?
additional information
?
-
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
lipoxygenase pathway
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
pathway of epidermal arachidonate oxygenation
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
lipoxygenase pathway
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
8-H(p)ETE is the major reaction product of 8-LOX independent of the pH
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
-
-
-
?
additional information
?
-
LOX1 has higher activity for eicosapentaenoic acid than arachidonic acid and docosahexaenoic acid
-
-
-
additional information
?
-
-
LOX1 has higher activity for eicosapentaenoic acid than arachidonic acid and docosahexaenoic acid
-
-
-
additional information
?
-
-
the inducible expression of 8-lipoxygenase inhibits cell growth, 15-LOX-2 and 8-LOX, although displaying different positional specificity, use common signaling pathways to induce growth inhibition in premalignant epithelial cells, overview
-
-
?
additional information
?
-
in the absence of arachidonate, Tyr181 and Arg182 of helix alpha2 participate in an interhelical charge cluster with Glu430 of the arched helix
-
-
?
additional information
?
-
-
usage of a combination of molecular dynamics simulations with quantum mechanics/molecular mechanics calculations to study the hydrogen abstraction step and the molecular oxygen addition step of the hydroperoxidation reaction of arachidonic acid catalyzed by both wild-type Coral 8R-LOX and its Gly427Ala mutant
-
-
?
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2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
arachidonate + O2
(5Z,9E,11Z,14Z)-(8S)-8-hydroperoxyeicosa-5,9,11,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8S)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
-
?
additional information
?
-
-
the inducible expression of 8-lipoxygenase inhibits cell growth, 15-LOX-2 and 8-LOX, although displaying different positional specificity, use common signaling pathways to induce growth inhibition in premalignant epithelial cells, overview
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
lipoxygenase pathway
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
pathway of epidermal arachidonate oxygenation
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
lipoxygenase pathway
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
2 arachidonic acid + 2 O2
8-hydroxy,9-oxo-eicosa-5Z,11Z,14Z-trienoic acid + 9-oxo-[8,12-cis]-prosta-5Z,10,14Z-trienoic acid + H2O
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
-
-
-
?
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arachidonate 8-lipoxygenase deficiency
Impaired Recovery from Influenza A/X-31(H3N2) Infection in Mice with 8-Lipoxygenase Deficiency.
Carcinogenesis
An antitumorigenic role for murine 8S-lipoxygenase in skin carcinogenesis.
Carcinogenesis
Constitutive expression of 8-lipoxygenase in papillomas and clastogenic effects of lipoxygenase-derived arachidonic acid metabolites in keratinocytes.
Carcinoma
An antitumorigenic role for murine 8S-lipoxygenase in skin carcinogenesis.
Carcinoma
Application of high-performance liquid chromatography-based analysis of DNA fragments to molecular carcinogenesis.
Carcinoma
Constitutive expression of 8-lipoxygenase in papillomas and clastogenic effects of lipoxygenase-derived arachidonic acid metabolites in keratinocytes.
Carcinoma
Elevated expression of 12/15-lipoxygenase and cyclooxygenase-2 in a transgenic mouse model of prostate carcinoma.
Carcinoma
Tumor-suppressive lipoxygenases inhibit the expression of c-myc mRNA coding region determinant-binding protein/insulin-like growth factor II mRNA-binding protein 1 in human prostate carcinoma PC-3 cells.
Carcinoma, Renal Cell
Application of high-performance liquid chromatography-based analysis of DNA fragments to molecular carcinogenesis.
Dehydration
Synthesis of 8,9-leukotriene A4 by murine 8-lipoxygenase.
Dermatitis
Upregulation of 8-lipoxygenase in the dermatitis of IkappaB-alpha-deficient mice.
Infections
Impaired Recovery from Influenza A/X-31(H3N2) Infection in Mice with 8-Lipoxygenase Deficiency.
Influenza, Human
Impaired Recovery from Influenza A/X-31(H3N2) Infection in Mice with 8-Lipoxygenase Deficiency.
Lung Neoplasms
The future of cyclooxygenase-2 inhibitors and other inhibitors of the eicosanoid signal pathway in the prevention and therapy of lung cancer.
Neoplasms
An antitumorigenic role for murine 8S-lipoxygenase in skin carcinogenesis.
Neoplasms
Application of high-performance liquid chromatography-based analysis of DNA fragments to molecular carcinogenesis.
Neoplasms
Characterization of an 8-lipoxygenase activity induced by the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate in mouse skin in vivo.
Neoplasms
Elevated expression of 12/15-lipoxygenase and cyclooxygenase-2 in a transgenic mouse model of prostate carcinoma.
Neoplasms
Phorbol ester induction of 8-lipoxygenase in inbred SENCAR (SSIN) but not C57BL/6J mice correlated with hyperplasia, edema, and oxidant generation but not ornithine decarboxylase induction.
Neoplasms
Proliferative responses of the skin to external stimuli.
Neoplasms
The future of cyclooxygenase-2 inhibitors and other inhibitors of the eicosanoid signal pathway in the prevention and therapy of lung cancer.
Papilloma
An antitumorigenic role for murine 8S-lipoxygenase in skin carcinogenesis.
Papilloma
Constitutive expression of 8-lipoxygenase in papillomas and clastogenic effects of lipoxygenase-derived arachidonic acid metabolites in keratinocytes.
Skin Diseases
Upregulation of 8-lipoxygenase in the dermatitis of IkappaB-alpha-deficient mice.
Tuberous Sclerosis
Application of high-performance liquid chromatography-based analysis of DNA fragments to molecular carcinogenesis.
Vaccinia
Site-directed mutagenesis studies on a putative fifth iron ligand of mouse 8S-lipoxygenase: retention of catalytic activity on mutation of serine-558 to asparagine, histidine, or alanine.
Whooping Cough
A pertussis toxin-sensitive 8-lipoxygenase pathway is activated by a nicotinic acetylcholine receptor in aplysia neurons.
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H604F
-
8-LOX mutant, induces strong pH-dependent alterations in the positional specificity but the pH-optimum remains the same. At acidic pH 8S-H(p)ETE is the exclusive arachidonic acid oxygenation product but with more alkaline pH increasing shares of 15S-H(p)ETE, above pH 9 15S-H(p)ETE is the major oxygenation product. Specific activity of 8-LOX mutant with (5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid as substrate continously declines when pH increases
Y603F
-
8-LOX mutant, is relative insensitive towards pH alterations in the near physiological range (pH 6-8), at strong alkaline conditions (pH more than 9) significant shares of 15S-H(p)ETE are formed
Y603F/H604F
-
8-LOX double mutant, induces strong pH-dependent alterations in the positional specificity but the pH-optimum remains the same. At acidic pH 8S-H(p)ETE is the exclusive arachidonic acid oxygenation product but with more alkaline pH increasing shares of 15S-H(p)ETE, above pH 9 15S-H(p)ETE is the major oxygenation product
A417G
-
converts arachidonic acid mainly to 12-hydroxyeicosatetraenoic acid, mutant retains 38% of catalytic efficiency
A417S
-
same oxygenase specificity and similar catalytic activity to wild-type 8S-LOX
A589M
site-directed mutagenesis, the mutant shows reduced activity and altered protein fold compared to the wild-type enzyme
A592M
stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A592M yields 19% 8R product, 2% 8S, 60% 11R, 4% 11S, plus some 12R/12S and 15R/15S product
A620H
site-directed mutagenesis, the mutant shows reduced activity and altered protein fold compared to the wild-type enzyme
A623H
stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A623H yields 16% 8R product, 4% 8S, 57% 11R, 5% 11S, 6% 12R, 6% 12S plus some 15R/15S product
D39A
-
118% activity compared to the wild type enzyme, mutant with diminished fluorescence resonance energy transfer properties, consistent with a role for calcium in membrane binding
D39A/E47A
-
106% activity compared to the wild type enzyme, a double mutant with calcium-binding residues from two of the three sites mutated exhibits no fluorescence resonance energy transfer signal
E47A
-
65% of the activity of the wild type enzyme, mutant with diminished fluorescence resonance energy transfer properties, consistent with a role for calcium in membrane binding
G427A
-
site-directed mutagenesis. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted
I433A
absence of the Ile side chain destabilizes the roof of the U-shaped channel, measurable activity only in the presence of CaCl2 and the detergent emolphogen
I433W
has no measurable activity, presumably because the Trp side chain effectively blocks the arachidonic acid binding site
L432A
less than 5% of the activity of the wild-type
L432F
less than 5% of the activity of the wild-type
L432I
less than 5% of the activity of the wild-type
L432V
less than 20% of the activity of the wild-type
L434F
mutation alters the regio- and stereospecificity of the final products, with a product ratio of 66 : 34 for 8R- and 12S-hydroperoxide, respectively. In the closed conformation, the phenyl group of Phe434 shields the C8 site of the substrate, preventing access of the oxygen molecule to this site, which leads to a quenching of the 8R-product. Both closed and open conformations of Phe434 allow the oxygen molecule to approach the pro-S face of the C12 site of the substrate, which enhances the propensity of the 12S-hydroperoxide
R182A
site-directed mutagenesis, the mutant shows reduced activity and altered protein fold compared to the wild-type enzyme
R185A
stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. R185A yields 87% 8R product, 2% 8S plus some 11R/11S, 12R/12S and 15R/15S product
W41A
-
140% activity compared to the wild type enzyme, exhibits only less than 2% of the increase in fluorescence at 517 nm upon the addition of CaCl2 of the wild-type signal
W77A
-
44% of the activity of the wild type enzyme, exhibits only 4% of the increase in fluorescence at 517 nm upon the addition of CaCl2 of the wild-type signal
additional information
-
doxycycline-inducible expression in keratinocytes 308 leads to an inhibition of cell growth that is associated with an inhibition of DNA synthesis, as shown by a reduction of 5-bromo-2-deoxy-uridine incorporation up to 46%, doxycycline-induced keratinocytes show increased levels of reactive oxygen species. The antioxidant N-acetyl-L-cysteine and a specific inhibitor of p38 mitogen-activated protein kinase, but not of extracellular signal-regulated kinase 1/2 or c-Jun N-terminal kinase/stress-activated kinases, completely abolish the LOX-induced growth inhibition
additional information
deletion mutant lacks one of the loops, as well as chelating amino acids from two of the three Ca2+ binding sites (the center site and that most distal from the catalytic domain). The Ca2+ site proximal to the catalytic domain, defined primarily by main chain contacts, remains intact and occupied in the mutant structure. Deletion mutant displays wild-type activity in a membrane-free assay, but Ca2+ does not promote membrane binding of the mutant and does not stimulate enzyme activity in a membrane-based assay
additional information
-
deletion mutant lacks one of the loops, as well as chelating amino acids from two of the three Ca2+ binding sites (the center site and that most distal from the catalytic domain). The Ca2+ site proximal to the catalytic domain, defined primarily by main chain contacts, remains intact and occupied in the mutant structure. Deletion mutant displays wild-type activity in a membrane-free assay, but Ca2+ does not promote membrane binding of the mutant and does not stimulate enzyme activity in a membrane-based assay
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Bundy, G.L.; Nidy, E.G.; Epps, D.E.; Mizsak, S.A.; Wnuk, R.J.
Discovery of an arachidonic acid C-8 lipoxygenase in the gorgonian coral Pseudoplexaura porosa
J. Biol. Chem.
261
747-751
1986
Pseudoplexaura porosa
brenda
Brash, A.R.; Baertschi, S.W.; Ingram, C.D.; Harris, T.M.
On non-cyclooxygenase prostaglandin synthesis in the sea whip coral, Plexaura homomalla: an 8(R)-lipoxygenase pathway leads to formation of an alpha-ketol and a Racemic prostanoid
J. Biol. Chem.
262
15829-15839
1987
Plexaura homomalla
brenda
Fuerstenberger, G.; Hagedorn, H.; Jacobi, T.; Besemfelder, E.; Stephan, M.; Lehman, W.D.; Marks, F.
Characterization of an 8-lipoxygenase activity induced by the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate in mouse skin in vivo
J. Biol. Chem.
266
15738-15745
1991
Mus musculus
brenda
Brash, A.R.; Boeglin, W.E.; Chang, M.S.; Shieh, B.H.
Purification and molecular cloning of an 8R-lipoxygenase from the coral Plexaura homomalla reveal the related primary structures of R- and S-lipoxygenases
J. Biol. Chem.
271
20949-20957
1996
Asteroidea, Callista chione, Plexaura homomalla, Strongylocentrotus purpuratus
brenda
Steel, D.J.; Tieman, T.L.; Schwartz, J.H.; Feinmark, S.L.
Identification of an 8-lipoxygenase pathway in nervous tissue of Aplysia californica
J. Biol. Chem.
272
18673-18681
1997
Aplysia californica
brenda
Qiao, N.; Takahashi, Y.; Takamatsu, H.; Yoshimoto, T.
Leukotriene A synthase activity of purified mouse skin arachidonate 8-lipoxygenase expressed in Escherichia coli
Biochim. Biophys. Acta
1438
131-139
1999
Mus musculus
brenda
Schneider, C.; Strayhorn, W.D.; Brantley, D.M.; Nanney, L.B.; Yull, F.E.; Brash, A.R.
Upregulation of 8-lipoxygenase in the dermatitis of IkB-a-deficient mice
J. Invest. Dermatol.
122
691-698
2004
Mus musculus
brenda
Coffa, G.; Brash, A.R.
A single active site residue directs oxygenation stereospecificity in lipoxygenases: Stereocontrol is linked to the position of oxygenation
Proc. Natl. Acad. Sci. USA
101
15579-15584
2004
Plexaura homomalla
brenda
Jisaka, M.; Iwanaga, C.; Takahashi, N.; Goto, T.; Kawada, T.; Yamamoto, T.; Ikeda, I.; Nishimura, K.; Nagaya, T.; Fushiki, T.; Yokota, K.
Double dioxygenation by mouse 8S-lipoxygenase: specific formation of a potent peroxisome proliferator-activated receptor alpha agonist
Biochem. Biophys. Res. Commun.
338
136-143
2005
Mus musculus
brenda
Oldham, M.L.; Brash, A.R.; Newcomer, M.E.
Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality
J. Biol. Chem.
280
39545-39552
2005
Plexaura homomalla
brenda
Schweiger, D.; Fuerstenberger, G.; Krieg, P.
Inducible expression of 15-lipoxygenase-2 and 8-lipoxygenase inhibits cell growth via common signaling pathways
J. Lipid Res.
48
553-564
2007
Mus musculus
brenda
Neau, D.B.; Gilbert, N.C.; Bartlett, S.G.; Boeglin, W.; Brash, A.R.; Newcomer, M.E.
The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity
Biochemistry
48
7906-7915
2009
Plexaura homomalla (O16025), Plexaura homomalla
brenda
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
Mus musculus
brenda
Saura, P.; Suardiaz, R.; Masgrau, L.; Gonzalez-Lafont, A.; Rosta, E.; Lluch, J.
Understanding the molecular mechanism of the Ala-versus-Gly concept controlling the product specificity in reactions catalyzed by lipoxygenases a combined molecular dynamics and QM/MM study of coral 8R-lipoxygenase
ACS Catal.
7
4854-4866
2017
Plexaura homomalla
-
brenda
Neau, D.B.; Bender, G.; Boeglin, W.E.; Bartlett, S.G.; Brash, A.R.; Newcomer, M.E.
Crystal structure of a lipoxygenase in complex with substrate the arachidonic acid-binding site of 8R-lipoxygenase
J. Biol. Chem.
289
31905-31913
2014
Plexaura homomalla (O16025)
brenda
Mishra, V.K.; Mishra, S.
Origin of regio- and stereospecific catalysis by 8-lipoxygenase
J. Phys. Chem. B
123
10605-10621
2019
Plexaura homomalla (O16025)
brenda
Gilbert, N.C.; Neau, D.B.; Newcomer, M.E.
Expression of an 8R-lipoxygenase from the coral Plexaura homomalla
Methods Enzymol.
605
33-49
2018
Plexaura homomalla (Q27901), Plexaura homomalla
brenda
Mishra, V.K.; Mishra, S.
Flipped regiospecificity in L434F mutant of 8-lipoxygenase
Phys. Chem. Chem. Phys.
22
16013-16022
2020
Plexaura homomalla (O16025)
brenda
Yuki, S.; Uemura, A.; Hakozaki, M.; Yano, A.; Abe, M.; Misawa, Y.; Baba, N.; Yamada, H.
Identification of a novel enzyme from E. pacifica that acts as an eicosapentaenoic 8R-LOX and docosahexaenoic 10R-LOX
Sci. Rep.
10
20592
2020
Euphausia pacifica (A0A7G1H6X8), Euphausia pacifica
brenda