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Information on EC 1.11.2.3 - plant seed peroxygenase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9CAB7
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1.11.2.3 plant seed peroxygenaseIUBMB Comments
A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin.
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Word Map
- 1.11.2.3
-
arachidonic
-
epoxyeicosatrienoic
- epoxide
- artery
-
cyclooxygenase
- lipoxygenase
-
vasodilation
- cyp2j2
-
eicosanoids
- indomethacin
-
hyperpolarizing
- miconazole
-
endothelium-derived
- 20-hete
-
dihydroxyeicosatrienoic
-
20-hydroxyeicosatetraenoic
-
ms-ppoh
-
cyp-derived
-
edhfs
-
arteriolar
-
endothelium-dependent
-
oleosins
-
nordihydroguaiaretic
-
vasodilatory
-
dhets
-
preglomerular
-
5,6-epoxyeicosatrienoic
-
large-conductance
- oxylipins
-
17-octadecynoic
-
eicosatetraynoic
-
cyp-dependent
- sulfaphenazole
-
hydroxyeicosatetraenoic
-
p450-derived
-
cross-recognition
- skf525a
-
regioisomeric
-
omega-hydroxylase
-
p450-dependent
-
14,15-epoxyeicosa-5z-enoic
-
11,12-epoxyeicosatrienoic
-
edhf-mediated
-
epoxygenation
-
5,8,11,14-eicosatetraynoic
-
laser-doppler
- cyp2c11
- aacocf3
-
iberiotoxin
-
17-odya
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
epoxygenase, caleosin, clo-3, cyp77b1, clo-1, clo/pxg, soybean peroxygenase, caleosin-like protein, caleosin/peroxygenase, hydroperoxide-dependent peroxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caleosin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
substrate:hydroperoxide oxidoreductase (RH-hydroxylating or epoxidising)
A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin.
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
linoleic acid + cumene hydroperoxide
?
-
64% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
-
?
linolenic acid + cumene hydroperoxide
linolenic acid 9,10-15,16-diepoxide + ?
74% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
major product, (R),(S)-epoxide enantiomers
-
?
13-hydroperoxyoctadecatrienoic acid + H2O2
13-hydroxyoctadecatrienoic acid + ?
-
-
-
?
13-hydroxyoctadecatrienoic acid + H2O2
15,16-epoxy-13-hydroperoxyoctadecadienoic acid + ?
-
-
-
?
2-hydroperoxyoctadecatrienoic acid + H2O2
2-hydroxyoctadecatrienoic acid + ?
-
-
-
?
aniline + cumene hydroperoxide
N-phenylhydroxylamine + H2O
-
-
-
?
linoleic acid + 13-hydroperoxy-9,11-octadecadienoic acid
?
13-hydroperoxy-9,11-octadecadienoic acid is the most active cosubstrate
-
-
?
linoleic acid + NADPH + H+
12,13-epoxy-octadec-cis-9-enoic acid + NADP+
-
-
-
-
?
linolenic acid + 13-hydroperoxy-9,11-octadecadienoic acid
?
13-hydroperoxy-9,11-octadecadienoic acid is the most active cosubstrate
-
-
?
oleic acid + 13-hydroperoxy-9,11-octadecadienoic acid
?
13-hydroperoxy-9,11-octadecadienoic acid is the most active cosubstrate
-
-
?
oleic acid + cumene hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
additional information
?
-
enzyme is an efficient fatty acid epoxygenase, catalyzing the oxidation of cis double bonds of unsaturated fatty acids. The C-12,13 double bond of these unsaturated fatty acids is the least favoured. Isoform PXG4 catalyzes exclusively the formation of (R),(S)-epoxide enantiomers, which is the absolute stereochemistry of the epoxides found in planta. Poor substrate: oleic acid methyl ester
-
-
?
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
linoleic acid + cumene hydroperoxide
?
-
64% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
-
?
linolenic acid + cumene hydroperoxide
linolenic acid 9,10-15,16-diepoxide + ?
74% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
major product, (R),(S)-epoxide enantiomers
-
?
13-hydroperoxyoctadecatrienoic acid + H2O2
13-hydroxyoctadecatrienoic acid + ?
-
-
-
?
13-hydroxyoctadecatrienoic acid + H2O2
15,16-epoxy-13-hydroperoxyoctadecadienoic acid + ?
-
-
-
?
2-hydroperoxyoctadecatrienoic acid + H2O2
2-hydroxyoctadecatrienoic acid + ?
-
-
-
?
oleic acid + cumene hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
additional information
?
-
enzyme is an efficient fatty acid epoxygenase, catalyzing the oxidation of cis double bonds of unsaturated fatty acids. The C-12,13 double bond of these unsaturated fatty acids is the least favoured. Isoform PXG4 catalyzes exclusively the formation of (R),(S)-epoxide enantiomers, which is the absolute stereochemistry of the epoxides found in planta. Poor substrate: oleic acid methyl ester
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
contains a protoheme of type b, with 0.6 nmol of heme per mg protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
the enzyme contains a Ca2+ binding motif, calcium is crucial for its peroxygenase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
the sulfoxidation of thiobenzamide, catalyzed by isoform PXG1, is completely abolished in the presence of 1 mM 2-mercaptoethanol (competitive inhibitor)
terbufos
-
a suicide substrate for plant peroxygenases, and at a concentration of 3 mM, it effectively inactivates the activity of isoform PXG1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
dominantly expressed in vascular bundles in most organs as well as in the guard cells
dominantly expressed in vascular bundles in most organs as well as in the guard cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
at the seed germination stage, a loss-of-function mutant is hypersensitive to abscisic acid, salt and mannitol stresses, whereas isoform CLO4-overexpressing lines are more hyposensitive to those stresses than the wild type. In adult stage, loss-of-function mutant and overexpressing plants show enhanced and decreased drought tolerance, respectively. Following exposure to exogenous abscisic acid, the expression of key abscisic acid-dependent regulatory genes, such as ABF3 and ABF4, is up-regulated in the loss-of-function mutant, while it is down-regulated in overexpressing lines
metabolism
peroxygenase CLO3 and alpha-dioxygenase together catalyze a coupling reaction to produce the antifungal compound 2-hydroxyoctadecanoic acid from alpha-linolenic acid
physiological function
physiological function
-
the membrane-bound isoform of caleosin plays a putative role as a peroxygenase involved in oxylipin metabolism during biotic and abiotic stress responses in Arabidopsis. Clo-3 is involved in the generation of oxidised fatty acids in stress-related signalling pathways involving both ABA and salicylic acid. Clo-3 is part of an oxylipin pathway induced by multiple stresses and may also generate fatty acid derived anti-fungal compounds for plant defence
physiological function
the enzyme is involved in the control of cell death during Arabidopsis responses to pathogens. Plants overexpressing the enzyme exhibit an alteration of their leaf cuticle wax components and an increased resistance to the pathogens Alternaria brassicicola or Pseudomonas syringae
physiological function
the enzyme mediates gibberellin-dependent flowering time, abscisic acid sensitivity, and tolerance to oxidative stress. The enzyme also confers tolerance against stress induced by Paraquat, Rose Bengal, heavy metal, and the synthetic auxins 1-naphthaleneacetic acid and 2,4-dichlorophenoxyacetic acid
physiological function
-
the enzyme interacts with the alpha subunit of the heterotrimeric G-protein complex in Arabidopsis and affects etiolation and leaf morphology. The enzyme plays a key role in the signaling pathway controlling hypocotyl length in dark grown seedlings and in leaf morphology
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). PXG4_ARATH
195
1
22092
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sumoylation
-
isoform PXG1 possesses a high sumoylation potentiality at the position Lys-196
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D70A
-
the disruption of calcium-binding in this mutant abolishes the interaction with the heterotrimeric G-protein complex GPA1. The mutant has altered leaf development
E81R
-
the disruption of calcium-binding in this mutant abolishes the interaction with the heterotrimeric G-protein complex GPA1. The mutant has altered leaf development
H138V
-
the mutant possess only 4% of the heme content wild type isoform PXG1
H70V
-
the heme content of the mutant is barely measurable (less than 1%) as compared to the wild type isoform PXG1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Trisacryl 300 gel filtration and CM-Sepharose column chromatography
-
nickel agarose bead chromatography and HiTrap Q FF Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaves and in Escherichia coli BL21 (DE3) cells
-
expressed in Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is down-regulated following exposure to exogenous abscisic acid and salt stress
isoform Clo-3 is highly upregulated following exposure to abiotic stresses, such as salt and drought or treatment with salicylic acid or 2,6-dichloroisonicotinic acid, and to biotic stress such as Leptosphaeria maculans infection
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hanano, A.; Burcklen, M.; Flenet, M.; Ivancich, A.; Louwagie, M.; Garin, J.; Blee, E.
Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif
J. Biol. Chem.
281
33140-33151
2006
Arabidopsis thaliana, Avena sativa
Partridge, M.; Murphy, D.J.
Roles of a membrane-bound caleosin and putative peroxygenase in biotic and abiotic stress responses in Arabidopsis
Plant Physiol. Biochem.
47
796-806
2009
Arabidopsis thaliana
Blee, E.; Flenet, M.; Boachon, B.; Fauconnier, M.L.
A non-canonical caleosin from Arabidopsis efficiently epoxidizes physiological unsaturated fatty acids with complete stereoselectivity
FEBS J.
279
3981-3995
2012
Arabidopsis thaliana (Q9CAB7)
Kim, Y.Y.; Jung, K.W.; Yoo, K.S.; Jeung, J.U.; Shin, J.S.
A stress-responsive caleosin-like protein, AtCLO4, acts as a negative regulator of ABA responses in Arabidopsis
Plant Cell Physiol.
52
874-884
2011
Arabidopsis thaliana (Q9CAB7)
Shimada, T.L.; Hara-Nishimura, I.
Leaf oil bodies are subcellular factories producing antifungal oxylipins
Curr. Opin. Plant Biol.
25
145-150
2015
Arabidopsis thaliana (O22788)
Blee, E.; Boachon, B.; Burcklen, M.; Le Guedard, M.; Hanano, A.; Heintz, D.; Ehlting, J.; Herrfurth, C.; Feussner, I.; Bessoule, J.J.
The reductase activity of the Arabidopsis caleosin RESPONSIVE TO DESSICATION20 mediates gibberellin-dependent flowering time, abscisic acid sensitivity, and tolerance to oxidative stress
Plant Physiol.
166
109-124
2014
Arabidopsis thaliana (O22788)
Hanano, A.; Bessoule, J.J.; Heitz, T.; Blee, E.
Involvement of the caleosin/peroxygenase RD20 in the control of cell death during Arabidopsis responses to pathogens
Plant Signal. Behav.
10
e991574
2015
Arabidopsis thaliana (O22788)
Brunetti, S.C.; Arseneault, M.K.M.; Wright, J.A.; Wang, Z.; Ehdaeivand, M.R.; Lowden, M.J.; Rivoal, J.; Khalil, H.B.; Garg, G.; Gulick, P.J.
The stress induced caleosin, RD20/CLO3, acts as a negative regulator of GPA1 in Arabidopsis
Plant Mol. Biol.
107
159-175
2021
Arabidopsis thaliana
Pineau, E.; Sauveplane, V.; Grienenberger, E.; Bassard, J.E.; Beisson, F.; Pinot, F.
CYP77B1 a fatty acid epoxygenase specific to flowering plants
Plant Sci.
307
110905
2021
Arabidopsis thaliana
Rahman, F.; Hassan, M.; Rosli, R.; Almousally, I.; Hanano, A.; Murphy, D.J.
Evolutionary and genomic analysis of the caleosin/peroxygenase (CLO/PXG) gene/protein families in the Viridiplantae
PLoS ONE
13
e0196669
2018
Arabidopsis thaliana, Auxenochlorella protothecoides, Capsaspora owczarzaki, Chlamydomonas reinhardtii, Chlorella variabilis, Chlorella vulgaris, Coccomyxa subellipsoidea, Gonium pectorale, Klebsormidium nitens, Marchantia polymorpha, Monoraphidium neglectum, Oryza sativa, Phoenix dactylifera, Physcomitrium patens, Selaginella moellendorffii, Sorangium cellulosum, Volvox carteri, Zea mays
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