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Information on EC 1.13.11.B6 - linoleate 9/13-lipoxygenase and Organism(s) Pisum sativum and UniProt Accession P09918

for references in articles please use BRENDA:EC1.13.11.B6
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Pisum sativum
UNIPROT: P09918 not found.
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Word Map
The taxonomic range for the selected organisms is: Pisum sativum
The enzyme appears in selected viruses and cellular organisms
Synonyms
oslox1, pnlox1, lox1:md:1a, 9/13-lipoxygenase, lox2:md:2a, 13/9-lox, linoleate 9 s-lipoxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9-/13-LOXN2
-
9/13-lipoxygenase
-
-
9/13-LOX
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
the reaction mechanism is different from LOX-2
linoleate + O2 = (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
reaction mechanism is different from LOX-3
SYSTEMATIC NAME
IUBMB Comments
lineate:oxygen 9/13-oxidoreductase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
the ratio of (9Z,11E)-13-hydroperoxy-11,13-octadecadienoate to (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is 1:2 for pea seed LOX-3 and recombinant LOX-3. The R/S stereoconfiguration of the products is not determined
-
?
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
linolenate + O2
?
show the reaction diagram
specific activity is 17% of the activity with linoleate. The R/S stereoconfiguration of the product is not determined
products not determined
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.7 - 6.9
linoleate
0.3 - 0.9
linoleate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65 - 78
linoleate
2 - 65
linoleate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.4 - 12.2
linoleate
6.7 - 74
linoleate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
recombinant enzyme
48
enzyme from pea seed
1.2
enzyme from pea seed
1.35
activity with linoleate
18
recombinant enzyme
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
L. cv. Bite
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOXN2 message is widespread in the cortex and endodermis of healthy roots, but specifically localized at high level in the cells bordering the nematode-induced syncytia of infected roots. In uninfected roots, the transcript is visualized in cortical and endodermal cells. In resistant infected roots, faint and infrequent signal spots are observed in the cortex, but LOXN2 message is abundant in the outer cells surrounding the vascular cylinder, in those cells injured by nematode penetration and those flanking the induced syncytia. In susceptible infected roots, the transcript is detected in cortical cells damaged by nematode invasion and undergoing necrosis, and in parenchymatous cells of the vascular cylinder strictly related to syncytia development
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
LOXN2 may be involved in late mechanisms of host resistance
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX3_PEA
861
0
97629
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
97000
x * 97000, SDS-PAGE
97134
x * 97134, calculated from sequence
100000
-
x * 100000, wild-type enzyme and mutant enzymes T579F, L569V and W523A, SDS-PAGE
94000
97628
x * 97628, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F580A
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%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hughes, R.K.; Wu, Z.; Robinson, D.S.; Hardy, D.; West, S.I.; Fairhurst, S.A.; Casey, R.
Characterization of authentic recombinant pea-seed lipoxygenases with distinct properties and reaction mechanisms
Biochem. J.
333
33-43
1998
Pisum sativum (P09918), Pisum sativum (P14856)
-
Manually annotated by BRENDA team
Hughes, R.K.; Lawson, D.M.; Hornostaj, A.R.; Fairhurst, S.A.; Casey, R.
Mutagenesis and modelling of linoleate-binding to pea seed lipoxygenase
Eur. J. Biochem.
268
1030-1040
2001
Pisum sativum
Manually annotated by BRENDA team
Veronico, P.; Giannino, D.; Melillo, M.T.; Leone, A.; Reyes, A.; Kennedy, M.W.; Bleve-Zacheo, T.
A novel lipoxygenase in pea roots. Its function in wounding and biotic stress
Plant Physiol.
141
1045-1055
2006
Pisum sativum (Q14ST9)
Manually annotated by BRENDA team