Information on EC 1.13.11.B6 - linoleate 9/13-lipoxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
linoleate 9/13-lipoxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
lineate:oxygen 9/13-oxidoreductase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Florunner
SwissProt
Manually annotated by BRENDA team
L. cv Mortarella
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
L., Leccino variety
UniProt
Manually annotated by BRENDA team
subsp. japonica, variety Beilu PL2
UniProt
Manually annotated by BRENDA team
cv. Desiree
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9E,11Z,15E)-octadeca-9,11,15-trienoic acid + O2
?
show the reaction diagram
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
(9S,10E,12Z)-9-hydroperoxy-octadeca-10,12-dienoate
show the reaction diagram
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
(9Z,12Z)-9-hydroxy-10-oxo-12-octadecenoic acid
show the reaction diagram
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoic acid + (9Z,12Z,15Z)-9-hydroxy-10-oxooctadeca-12,15-dienoic acid
show the reaction diagram
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
show the reaction diagram
1,2-di-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + O2
?
show the reaction diagram
low activity with the wild-type enzyme, no activity with mutant A562G
-
-
?
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2
?
show the reaction diagram
all-cis-9,12,15-octadecatrienoic acid + O2
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid + 9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
show the reaction diagram
all-cis-9,12-octadecadienoic acid + O2
9-hydroxy-10-oxo-12Z-octadecenoic acid
show the reaction diagram
-
i.e. linoleic acid
the alpha-ketol is the main metabolite formed from 9R-hydroperoxyoctadecadienoic acid
-
?
arachidonate + O2
?
show the reaction diagram
specific activity is 13% of the activity with linoleate
products not determined
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
the enzyme delivers a 50:50 mixture of (9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate, with higher turn out of R stereoisomers over S isomers (60:40)
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
the catalytic efficiency of the recombinant olive LOX was significantly higher for linoleic acid hydroperoxidation than for linolenic acid hydroperoxidation
dual positional specificity: the enzyme forms (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate in a 2:1 ratio, the products are predominantly in 9S and 13R configuration
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
linoleate + O2
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate
show the reaction diagram
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
?
linolenate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
the enzyme forms (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate and (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate in a 6:4 ratio. The R/S stereoconfiguration of the products is not determined
-
?
linolenate + O2
?
show the reaction diagram
monolinolenoylglycerol + O2
?
show the reaction diagram
phosphorylcholine + O2
?
show the reaction diagram
activity with the wild-type enzyme, no activity with mutant A562G
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
(9Z,12Z)-9-hydroxy-10-oxo-12-octadecenoic acid
show the reaction diagram
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoic acid + (9Z,12Z,15Z)-9-hydroxy-10-oxooctadeca-12,15-dienoic acid
show the reaction diagram
all-cis-9,12,15-octadecatrienoic acid + O2
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid + 9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
show the reaction diagram
all-cis-9,12-octadecadienoic acid + O2
9-hydroxy-10-oxo-12Z-octadecenoic acid
show the reaction diagram
-
i.e. linoleic acid
the alpha-ketol is the main metabolite formed from 9R-hydroperoxyoctadecadienoic acid
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
Q9AXG8
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
Q27PX2
-
the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is 4:3
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Q9AXG8
-
-
-
?
additional information
?
-
-
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
Mn:Fe ratio is 1:0.05
Mn2+
-
manganese 9S-lipoxygenase, 9S-LOX contains catalytic manganese, Mn:protein ratio is about 0.2:1, while the Mn:Fe ratio is 1:0.05
additional information
-
the catalytic metal of the 9S-LOX is manganese and not iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-cyclodextrin
-
-
nordihydroguaiaretic acid
noncompetitive
propyl gallate
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
(9Z,12Z)-octadeca-9,12-dienoic acid
-
pH 9.0, 22C
0.175 - 6.9
linoleate
0.344
linolenate
25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.3
(9Z,12Z)-octadeca-9,12-dienoic acid
Nakataea oryzae
-
pH 9.0, 22C
2 - 106
linoleate
47.8
linolenate
Olea europaea
B6D1W5
25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
(9Z,12Z)-octadeca-9,12-dienoic acid
Nakataea oryzae
-
pH 9.0, 22C
8792
6.7 - 530
linoleate
808
139
linolenate
Olea europaea
B6D1W5
25C
5572
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00409
nordihydroguaiaretic acid
25C
0.00188
propyl gallate
25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.2
enzyme from pea seed
1.35
activity with linoleate
18
recombinant enzyme
40
recombinant enzyme
48
enzyme from pea seed
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 6.5
enzyme from pea seed
5.7 - 6.7
recombinant enzyme
5.8 - 6.4
recombinant enzyme and enzyme from pea seed
9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
pH 4.5: about 45% of maximal actvity, pH 7.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.95
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
constitutively expressed in cotyledons of immature seeds, no expression in untreated mature seeds
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
detected in all olive developmental and ripening stages from green small fruits to black or senescent fruits. Mainly expressed at late developmental stages
Manually annotated by BRENDA team
potato 13/9-LOX is only a minor component of the total LOX population in tubers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
likely confined to the cytosol, because it contains neither consensus targeting nor retention signals for any organelles
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparison of the structure of lipoxygenase L3 with its L1 isoenzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
9S-LOX activity is less robust during expression and purification, possibly due to proteolysis, stability is not improved by addition of 0.001 mM pepstatin A, 0.001 mM leupeptin, or 1 mM EDTA to the growth medium
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified recombinant 9S-MnLOX can be stored for several weeks at 4C with retained activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Pichia pastoris by hydrophobic interaction chromatography, dialfiltration, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a His-tagged fusion protein in Escherichia coli
expression in Escherichia col BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
expression in Pichia pastoris
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS
recombinant expression in Pichia pastoris
-
sequence comparison and homology modelling
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LOXN2 transcription is monitored in roots after mechanical injury and during nematode infection. The message peaks at 3 and 24 h after wounding in both genotypes and is more abundant in the resistant than in the susceptible pea. In nematode-infected roots, transcription of several LOX genes is triggered except LOXN2, which is repressed in both genotypes
PnLOX1 expression is induced by wounding, methyl jasmonate and Aspergillus infection in mature seed
transformants with a lower level of OsLOX1 expression are less able to tolerate brown planthopper attack
transformants with enhanced level of OsLOX1 expression are more resistant to brown planthopper attack
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q599F
the wild-type enzyme is a linoleate 13-LOX above pH 7.5, below this value it functions as a linoleate 9-LOX. The mutant loses its 13-LOX activity at higher pH-values. At pH-values above 7.5 a rather unspecific product pattern (1:1 ratio of 13-hydroperoxy-(10E,12Z)-octadecadienoate and 9-hydroperoxy-(10E,12Z)-octadecadienoate) is observed with the mutant enzyme. The unspecific oxygenation reaction is also indicated by the R/S-ratio (4:6) of the major reaction products
Q599H
the mutation converts the enzyme to a linoleate 13-LOX lacking any pH sensitivity. The pH optimum remains unaffected, and the major product isomers are in the S-configuration
F580A
-
kcat/KM for linoleate hydroperoxidation is increased by 35%; possesses activity profile that is similar to wild-type
F580V
-
possesses activity profile that is similar to wild-type
K578/T579RS
-
possesses activity profile that is similar to wild-type
L569V
-
kcat/KM for linoleate hydroperoxidation is reduced by 38%
T579F
-
kcat/KM for linoleate hydroperoxidation is reduced by 89%
T579S
-
possesses activity profile that is similar to wild-type
V570I
-
possesses activity profile that is similar to wild-type
W523A
-
kcat/KM for linoleate hydroperoxidation is reduced by 98%
I437L
KM-value for linoleate is 114% of wild-type value, kcat/Km for linoleate is 83% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.7 (compared to 0.8 in reaction with wild-type enzyme)
V570I
KM-value for linoleate is 61% of wild-type value, kcat/Km for linoleate is 367% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.6 (compared to 0.8 in reaction with wild-type enzyme)
V580F
KM-value for linoleate is 384% of wild-type value, kcat/Km for linoleate is 4% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.9 (compared to 0.8 in reaction with wild-type enzyme)
additional information