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Information on EC 1.13.11.40 - arachidonate 8-lipoxygenase
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1.13.11.40 arachidonate 8-lipoxygenaseIUBMB Comments
From the coral Pseudoplexaura porosa.
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Word Map
- 1.13.11.40
- lipoxygenases
-
coral
-
allene
-
plexaura
- homomalla
-
8r-hpete
-
epidermis-type
-
whip
- 12r-lox
-
8-hydroxyeicosatetraenoic
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
8-lipoxygenase, 8-lox, 8r-lipoxygenase, 8s-lox, 8r-lox, 8s-lipoxygenase, 8(r)-lipoxygenase, arachidonate 8-lipoxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
8(R)-lipoxygenase
-
-
-
-
8-lipoxygenase
8R-lipoxygenase
8R-LOX
8-lipoxygenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
arachidonate + O2 = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
from the coral Pseudoplexaura porosa
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dioxygenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
arachidonate:oxygen 8-oxidoreductase
From the coral Pseudoplexaura porosa.
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CAS REGISTRY NUMBER
COMMENTARY
100900-72-9
-
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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
(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
-
-
-
-
?
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
?
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)
-
-
?
docosahexaenoic acid + O2
10R-hydroxy-docosahexaenoic acid
-
-
-
?
eicosapentaenoic acid + O2
8R-hydroxy-eicosapentaenoic 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
-
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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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
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)-(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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
the catalytic iron in 8R-LOX is positioned by three invariant His384, His389, and His570 side chains and the terminal main chain. Fe2+ sits in the base of a large U-shaped cavity, positioned by invariant Leu385 on one side, and the iron and His384 and His389 on the other. Leu385 and the catalytic iron cradle the base of the U
Iron
during the hydrogen abstraction step, the hydroxyl group bound to the metal center activates the C-H bond of the double-allylic carbon center of the substrate that leads to the formation of a radical center at the substrate
Ca2+
has three Ca2+ binding sites flanked by putative membrane insertion loops in the C2-like domain
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
physico-chemical state of the substrate and the complex equilibrium between fatty acid monomers, acid soaps and micelles may impact the reaction specificity of LOX-isoforms
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
arachidonate 8-lipoxygenase deficiency
Impaired Recovery from Influenza A/X-31(H3N2) Infection in Mice with 8-Lipoxygenase Deficiency.
Carcinogenesis
Constitutive expression of 8-lipoxygenase in papillomas and clastogenic effects of lipoxygenase-derived arachidonic acid metabolites in keratinocytes.
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.
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
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
The future of cyclooxygenase-2 inhibitors and other inhibitors of the eicosanoid signal pathway in the prevention and therapy of lung cancer.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.039
(15S)-hydroperoxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
0.015
(15S)-hydroxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
0.0021
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
0.0057
(8S)-hydroxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
additional information
additional information
substrate inhibition steady state kinetics
-
0.03
arachidonate
recombinant His-tagged wild-type enzyme, pH 7.4, 22°C
0.058
arachidonate
recombinant His-tagged mutant A620H, pH 7.4, 22°C
0.059
arachidonate
recombinant His-tagged mutant A589M, pH 7.4, 22°C
0.067
arachidonate
recombinant His-tagged mutant R182A, pH 7.4, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
(15S)-hydroperoxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
1
(15S)-hydroxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
7
(8R)-8-hydroperoxy-5,9,11,14-eicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
3.5
(8S)-hydroxyeicosatetraenoic acid
-
in 50 mM sodium phosphate buffer, pH 7.4, at 25°C
210
arachidonate
recombinant His-tagged wild-type enzyme, pH 7.4, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
55.2
arachidonate
recombinant His-tagged mutant A620H, pH 7.4, 22°C
542.4
arachidonate
recombinant His-tagged mutant A589M, pH 7.4, 22°C
2880.6
arachidonate
recombinant His-tagged mutant R182A, pH 7.4, 22°C
7000
arachidonate
recombinant His-tagged wild-type enzyme, pH 7.4, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity of 8-LOX with (5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid as substrate strongly increases going from pH 6 to 7.2 but then drops down at more alkaline pH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional allene oxide synthase-lipoxygenase protein
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
increased expression of 8-LOX in stratum granulosum of IkappaB-alpha-deficient mice
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the mechanism consists of hydrogen abstraction from one double allylic carbon atom of substrate followed by oxygen insertion at the resulting prochiral carbon radical of the substrate. The positional specificity of the hydrogen abstraction is a result of conformational dynamics of the bound substrate. The C10 atom of the substrate is the most probable site of hydrogen abstraction in wild-type. The dominating 8R product in the wild-type is due to the presence of the aromatic ring pairs of Tyr181 and Phe173 acting as a gatekeeper for efficient delivery of oxygen at the pro-R face of C8
physiological function
-
lipoxygenases (LOXs) are a family of enzymes that catalyze the highly specific hydroperoxidation of polyunsaturated fatty acids, such as arachidonic acid. Different stereo- or/and regioisomer hydroperoxidation products lead later to different metabolites that exert opposite physiological effects in the animal body and play a central role in inflammatory processes. The Gly-Ala switch of a single residue is crucial for the stereo- and regiocontrol in many lipoxygenases
additional information
additional information
-
molecular dynamics simulations, quantum mechanics/molecular mechanics calculations, overview. 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
additional information
subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation, both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery, modeling, overview
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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). AOSL_PLEHO
1066
0
121783
Swiss-Prot
other Location (Reliability: 1)
L0B198_THEEQ
1242
0
137099
TrEMBL
Secretory Pathway (Reliability: 2)
S2DJI8_INDAL
Indibacter alkaliphilus (strain CCUG 57479 / KCTC 22604 / LW1)
332
0
38814
TrEMBL
-
A0A7G1H6X8_9EUCA
691
0
79408
TrEMBL
Mitochondrion (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
-
mature protein predicted from the cDNA, difference from the size estimated by SDS-PAGE implies a post-translational modification of the enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY