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Information on EC 1.13.11.92 - fatty acid alpha-dioxygenase
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EC Tree
1.13.11.92 fatty acid alpha-dioxygenaseIUBMB Comments
Contains heme. This plant enzyme catalyses the (2R)-hydroperoxidation of fatty acids. It differs from lipoxygenases and cyclooxygenases in that the oxygen addition does not target an unsaturated region in the fatty acid. In vitro the product undergoes spontaneous decarboxylation, resulting in formation of a chain-shortened aldehyde. In vivo the product may be reduced to a (2R)-2-hydroxyfatty acid. The enzyme, which is involved in responses to different abiotic and biotic stresses, has a wide substrate range that includes both saturated and unsaturated fatty acids.
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Word Map
- 1.13.11.92
- oxylipins
-
pathogen-induced
-
sexta
-
patens
-
manduca
-
botrytis
-
cinerea
-
herbivory
- polygalacturonase
-
physcomitrella
-
attenuata
-
moss
- synthesis
-
turnera
-
alpha-oxidation
-
endoperoxide
-
lipoxygenase-generated
-
defense-related
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
=
a (2R)-2-hydroperoxyfatty acid
Synonyms
alpha-dioxygenase, alpha-dox1, padox-1, fatty acid alpha-dioxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DOX1
-
-
-
-
Piox
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fatty acid + O2 = a (2R)-2-hydroperoxyfatty acid
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
fatty acid:oxygen 2-oxidoreductase [(2R)-2-hydroperoxyfatty acid-forming]
Contains heme. This plant enzyme catalyses the (2R)-hydroperoxidation of fatty acids. It differs from lipoxygenases and cyclooxygenases in that the oxygen addition does not target an unsaturated region in the fatty acid. In vitro the product undergoes spontaneous decarboxylation, resulting in formation of a chain-shortened aldehyde. In vivo the product may be reduced to a (2R)-2-hydroxyfatty acid. The enzyme, which is involved in responses to different abiotic and biotic stresses, has a wide substrate range that includes both saturated and unsaturated fatty acids.
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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
10-methyldodecanoic acid + O2
(2R)-10-methyl-2-hydroperoxy-dodecanoic acid
-
-
-
?
11-methyldodecanoic acid + O2
(2R)-11-methyl-2-hydroperoxy-dodecanoic acid
-
-
-
?
11-methyltridecanoic acid + O2
(2R)-11-methyl-2-hydroperoxy-tridecanoic acid
-
-
-
?
12-methyltridecanoic acid + O2
(2R)-12-methyl-2-hydroperoxy-tridecanoic acid
-
-
-
?
13-methylpentadecanoic acid + O2
(2R)-13-methyl-2-hydroperoxy-pentadecanoic acid
-
-
-
?
13-methyltetradecanoic acid + O2
(2R)-13-methyl-2-hydroperoxy-tetradecanoic acid
-
-
-
?
14-methylpentadecanoic acid + O2
(2R)-14-methyl-2-hydroperoxy-pentadecanoic acid
-
-
-
?
3-thiamyristate + O2
(2R)-2-hydroperoxy-3-thiatetradecanoic acid
-
-
-
?
arachidonic acid + O2
(4Z,7Z,10Z,13Z)-nonadeca-5,8,11,14-trienal + (2R)-2-hydroxy-(5Z,8Z,11Z,14Z)-eicosa-5,8,11,14-trienoic acid + (4Z,7Z,10Z,13Z)-nonadeca-4,7,10,13-tetraenoic acid + CO2
O82031
-
-
-
?
hexadecanoic acid + O2
(2R)-2-hydroperoxy-hexadecanoic acid
-
more than 99% enantiomeric excess
-
-
?
linoleic acid + O2
(8Z,11Z)-heptadeca-8,11-dienal + (2R)-2-hydroxy-(9Z,12Z)-octadeca-9,12-dienoic acid + (8Z,11Z)-heptadeca-8,11-dienoic acid + CO2
linolenic acid + O2
(8Z,11Z,14Z)-heptadeca-8,11,14-trienal + (2R)-2-hydroxy-(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + (8Z,11Z,14Z)-heptadeca-8,11,14-trienoic acid + CO2
oleic acid + O2
(8Z)-heptadeca-8-enal + (2R)-2-hydroxy-(9Z)-octadeca-9-enoic acid + (8Z)-heptadeca-8-enoic acid + CO2
linoleic acid + O2
(2R)-2-hydroperoxy-(9Z,12Z)-octadeca-9,12-dienoic acid
-
-
-
?
linoleic acid + O2
(2R)-2-hydroperoxy-(9Z,12Z)-octadeca-9,12-dienoic acid
-
-
-
?
linoleic acid + O2
(2R)-2-hydroperoxy-(9Z,12Z)-octadeca-9,12-dienoic acid
-
-
-
-
?
linoleic acid + O2
(8Z,11Z)-heptadeca-8,11-dienal + (2R)-2-hydroxy-(9Z,12Z)-octadeca-9,12-dienoic acid + (8Z,11Z)-heptadeca-8,11-dienoic acid + CO2
-
-
-
-
?
linoleic acid + O2
(8Z,11Z)-heptadeca-8,11-dienal + (2R)-2-hydroxy-(9Z,12Z)-octadeca-9,12-dienoic acid + (8Z,11Z)-heptadeca-8,11-dienoic acid + CO2
O82031
-
-
-
?
linolenic acid + O2
(2R)-2-hydroperoxy-(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
-
-
?
linolenic acid + O2
(2R)-2-hydroperoxy-(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
-
-
?
linolenic acid + O2
(8Z,11Z,14Z)-heptadeca-8,11,14-trienal + (2R)-2-hydroxy-(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + (8Z,11Z,14Z)-heptadeca-8,11,14-trienoic acid + CO2
-
-
-
-
?
linolenic acid + O2
(8Z,11Z,14Z)-heptadeca-8,11,14-trienal + (2R)-2-hydroxy-(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + (8Z,11Z,14Z)-heptadeca-8,11,14-trienoic acid + CO2
O82031
-
-
-
?
myristic acid + O2
(2R)-2-hydroperoxy-tetradecanoic acid
-
-
-
?
myristic acid + O2
(2R)-2-hydroperoxy-tetradecanoic acid
-
-
-
?
oleic acid + O2
(2R)-2-hydroperoxy-(9Z)-octadeca-9-enoic acid
-
-
-
?
oleic acid + O2
(2R)-2-hydroperoxy-(9Z)-octadeca-9-enoic acid
-
-
-
?
oleic acid + O2
(8Z)-heptadeca-8-enal + (2R)-2-hydroxy-(9Z)-octadeca-9-enoic acid + (8Z)-heptadeca-8-enoic acid + CO2
-
-
-
-
?
oleic acid + O2
(8Z)-heptadeca-8-enal + (2R)-2-hydroxy-(9Z)-octadeca-9-enoic acid + (8Z)-heptadeca-8-enoic acid + CO2
O82031
-
-
-
?
palmitic acid + O2
pentadecanal + 2-hydroxyhexadecanoic acid + pentadecanoic acid + CO2
-
-
-
-
?
palmitic acid + O2
pentadecanal + 2-hydroxyhexadecanoic acid + pentadecanoic acid + CO2
O82031
-
-
-
?
additional information
?
-
no substrates: methyl esters of myristate, linoleate and linolenate are not oxygenated
-
-
-
additional information
?
-
-
enzyme shows both peroxidase and NAD+ oxidoreductase activity
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
1 mol of heme bound tightly but noncovalently per protein monomer. The high spin ferric heme can be reduced to the ferrous state by dithionite
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,4-dehydromyristate
inactivates the oxygenase without appreciable oxygen consumption
Zn2+
presence of Zn2+ does not change the Km values for linoleate or oxygen, or the Ki value for cyanide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacterial Infections
Activation of the fatty acid alpha-dioxygenase pathway during bacterial infection of tobacco leaves. Formation of oxylipins protecting against cell death.
Bacterial Infections
Involvement of the Arabidopsis alpha-DOX1 fatty acid dioxygenase in protection against oxidative stress and cell death.
Infections
Activation of the fatty acid alpha-dioxygenase pathway during bacterial infection of tobacco leaves. Formation of oxylipins protecting against cell death.
Infections
Functional analysis of {alpha}-DOX2, an active {alpha}-dioxygenase critical for normal development in tomato plants.
Infections
Involvement of the Arabidopsis alpha-DOX1 fatty acid dioxygenase in protection against oxidative stress and cell death.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
during germination, alpha-dioxygenase mRNA accumulates in the cotyledons and the embryonic axis of pea seeds de novo. alpha-Dioxygenase enzymatic activity in plant extracts is highest in cotyledons during imbibition
brenda
during germination, alpha-dioxygenase mRNA accumulates in the cotyledons and the embryonic axis of pea seeds de novo
brenda
additional information
in developing pea plants, the transcript is detected almost exclusively in roots
brenda
additional information
gene expression is confined to necrotic lesions during the hypersensitive response to bacterial infections, it occurs throughout the chlorotic area during a compatible interaction. Accumulation of alpha-DOX1 transcripts is impaired in salicylic acid-compromised plants and induced by salicylic acid and by chemicals generating nitric oxide, intracellular superoxide or singlet oxygen
brenda
additional information
the accumulation of alpha-dioxygenase protein parallels transcript accumulation in that it is abundant in germinating as well as young plant tissue, and correlates with loss of mRNA during plant maturation
brenda
additional information
-
the accumulation of alpha-dioxygenase protein parallels transcript accumulation in that it is abundant in germinating as well as young plant tissue, and correlates with loss of mRNA during plant maturation
brenda
additional information
alpha-DOX1 transcripts are detected in the roots and absent in all other organs
brenda
additional information
-
alpha-DOX1 transcripts are detected in the roots and absent in all other organs
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
2-hydroxylinolenic acid, produced by attack-activated alpha-DOX1 activity, participates in defense activation during insect feeding. Attack by Manduca sexta larvae amplifies 2-hydroxylinolenic acid formation at the feeding sites. Manduca sexta larvae perform better on alpha-Dox1-silenced plants than on wildtype plants. Repeated applications of 2-hydroxylinolenic acid to wounds before insect feeding partly amplifies jasmonic acid-controlled defenses and restores the resistance of alpha-Dox1-silenced plants
physiological function
O82031
alpha-dioxygenase-generated 2-hydroxylinolenic acid, and to a lesser extent lipoxygenase-generated 9-hydroxyoctadecatrienoic acid, exert a tissue-protective effect in bacterially infected tobacco leaves. In transgenic tobacco plants overexpressing alpha-dioxygenase, incompatible infection of leads to a dramatic elevation of 2-hydroxylinolenic acid and 8,11,14-heptadecatrienoic acid, whereas the levels of lipoxygenase products are strongly decreased
physiological function
alpha-DOX1 gene contributes to defense responses against aphids. Green peach aphid population growth on an alpha-DOX1 T-DNA insertion lines is approximately 25% higher as compared with corresponding wild-type
physiological function
-
down-regulation of alphaDOX enhances susceptibility to bacterial pathogens and suppresses the hypersensitive response via the suppression of pathogenesis-related genes such as PR4, proteinase inhibitor II and lipid transfer protein PR14. alpha-DOX-silenced pepper plants also exhibit more retarded growth with lower epidermal cell numbers and reduced cell wall thickness than control plants
physiological function
transgenic plants with altered levels of alpha-DOX1 react like wild-type plants to a compatible pathogen. Plants with reduced activity develop a more rapid and severe necrotic response than wild-type plants to incompatible bacteria and paraquat treatment, respectively, and a milder response when alpha-DOX1 is overproduced
physiological function
virus-induced gene silencing of isoform alpha-DOX1 enhances aphid Macrosiphum euphorbiae population growth in wild-type plants. An even higher enhancement in aphid numbers occurs when alpha-DOX1 is silenced in spr2, a mutant line characterized by elevated linoleic acid levels, decreased linolenic acid levels, and enhanced aphid resistance as compared with wild-type
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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). PIOX_ORYSJ
618
0
70441
Swiss-Prot
other Location (Reliability: 2)
PIOX_PEA
643
0
73297
Swiss-Prot
other Location (Reliability: 2)
PIOX_TOBAC
643
0
73453
Swiss-Prot
other Location (Reliability: 2)
DOX1_ARATH
639
0
73158
Swiss-Prot
Secretory Pathway (Reliability: 2)
B1WSS6_CROS5
Crocosphaera subtropica (strain ATCC 51142 / BH68)
613
0
70481
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
PADOX1 cleaved from GST-PADOX1 fusion by thrombin forms large multimeric complexes of 6-10 monomers. Full length PADOX1 expressed via a pCW vector in bacteria is a tetramer. Full length PADOX1 expressed in Sf9 cells chromatographed as a monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure to 1.5 A resolution. The structure is monomeric, predominantly helical-helical, and comprised of two domains. Helices H2, H6, H8, and H17 form the heme binding cleft and walls of the active site channel. Residues His318, Thr323, and Arg566 are located near the catalytic tyrosine, Tyr386, at the apex of the channel, where they interact with a chloride ion. Two extended inserts are present on the surface of the enzyme that restrict access to the distal face of the heme
structures of wild-type in complex with H2O2, and the catalytically inactive Y379F mutant in complex with palmitic acid. PA binds within the active site cleft of alpha-DOX such that the carboxylate forms ionic interactions with residues His311 and Arg559. Thr316 aids in the positioning of carbon-2 for hydrogen abstraction. The binding of H2O2 at the distal face of the heme displaces residues His157, Asp158, and Trp159 about 2.5 A from their positions in the wild type structure
Q9M5J1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H163C
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H163E
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H163M
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H163Y
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H389C
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H389E
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H389M
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
H389Y
mutation results in perturbation of the heme absorbance spectrum and oxygenase activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from germinating pea, using (NH4)2SO4 and pH precipitations and three successive chromatographic steps
-
recombinant protein
recombinant protein, purification by Protino nickel-nitrilotriacetic acid agarose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethylene down-regulates the DOX expression and also the endogenous level of jasmonic acid in rice seedlings
Q9M5J1
expression in root is enhanced by by salt, wounding, abscisic acid and challenge with Pythium aphanidermatum. Ethylene-generating agent ethephon and precursor 1-aminocyclopropane-1-carboxylic acid markedly elevate DOX1 expression, and this enhanced expression is suppressed by abscisic acid
expression of isoform alpha-DOX1 gene is induced in response to both incompatible and compatible bacterial infections. The level of alpha-DOX1 mRNA and dioxygenase activity appears earlier and reaches higher values when infection promotes a hypersensitive reaction
potato aphid Macrosiphum euphorbiae induces isoform alpha-DOX1 but not alpha-DOX2 expression in tomato. alpha-DOX1 upregulation by aphids does not require either jasmonic acid or salicylic acid accumulation
rice blight bacteria, Xanthomonas oryzae, elicits the accumulation of alpha-DOX transcripts in the leaves in both the incompatible and compatible interactions. Treating the seedling with CuSO4 also significantly enhances the DOX expression. The degree of induction is mostly parallel to the level of endogenous jasmonic acid in the leaves
Q9M5J1
potato aphid Macrosiphum euphorbiae induces isoform alpha-DOX1 but not alpha-DOX2 expression in tomato. alpha-DOX1 upregulation by aphids does not require either jasmonic acid or salicylic acid accumulation
potato aphid Macrosiphum euphorbiae induces isoform alpha-DOX1 but not alpha-DOX2 expression in tomato. alpha-DOX1 upregulation by aphids does not require either jasmonic acid or salicylic acid accumulation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
biotechnological production of C12-C15 branched-chain fatty aldehydes. The enzyme efficiently transforms short-chained fatty acids. The transformation products (C12-C15 iso- and anteisoaldehydes) exhibit green-soapy, sweety odors with partial citrus-like, metallic, peppery, and savory-tallowy nuances
synthesis
-
synthesis of fatty aldehydes based on Escherichia coli cells expressing alpha-dioxygenase from Oryza sativa. In resting cells of recombinant Escherichia coli, conversion of different fatty acids to the respective fatty aldehydes shortened by one carbon atom is demonstrated. The usage of Triton X 100 improves the conversion rate up to 1 g aldehyde per liter per hour
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaehne, F.; Buchhaupt, M.; Schrader, J.
A recombinant alpha-dioxygenase from rice to produce fatty aldehydes using E. coli
Appl. Microbiol. Biotechnol.
90
989-995
2011
Oryza sativa
brenda
Goulah, C.C.; Zhu, G.; Koszelak-Rosenblum, M.; Malkowski, M.G.
The crystal structure of alpha-dioxygenase provides insight into diversity in the cyclooxygenase-peroxidase superfamily
Biochemistry
52
1364-1372
2013
Arabidopsis thaliana (Q9SGH6)
brenda
Hammer, A.; Albrecht, F.; Hahne, F.; Jordan, P.; Fraatz, M.; Ley, J.; Geissler, T.; Schrader, J.; Zorn, H.; Buchhaupt, M.
Biotechnological production of odor-active methyl-branched aldehydes by a novel alpha-dioxygenase from Crocosphaera subtropica
J. Agric. Food Chem.
68
10432-10440
2020
Crocosphaera subtropica (B1WSS6)
-
brenda
Hamberg, M.; Sanz, A.; Castresana, C.
alpha-Oxidation of fatty acids in higher plants. Identification of a pathogen-inducible oxygenase (piox) as an alpha-dioxygenase and biosynthesis of 2-hydroperoxylinolenic acid
J. Biol. Chem.
274
24503-24513
1999
Arabidopsis thaliana, Nicotiana tabacum (O82031), Nicotiana tabacum
brenda
Hamberg, M.; Sanz, A.; Rodriguez, M.J.; Calvo, A.P.; Castresana, C.
Activation of the fatty acid alpha-dioxygenase pathway during bacterial infection of tobacco leaves. Formation of oxylipins protecting against cell death
J. Biol. Chem.
278
51796-51805
2003
Nicotiana tabacum (O82031), Nicotiana tabacum
brenda
Liu, W.; Rogge, C.E.; Bambai, B.; Palmer, G.; Tsai, A.L.; Kulmacz, R.J.
Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-dioxygenase-1
J. Biol. Chem.
279
29805-29815
2004
Arabidopsis thaliana (A0A178V8W6), Arabidopsis thaliana
brenda
Tirajoh, A.; Aung, T.S.; McKay, A.B.; Plant, A.L.
Stress-responsive alpha-dioxygenase expression in tomato roots
J. Exp. Bot.
56
713-723
2005
Solanum lycopersicum (Q69F00), Solanum lycopersicum
brenda
Koeduka, T.; Matsui, K.; Hasegawa, M.; Akakabe, Y.; Kajiwara, T.
Rice fatty acid alpha-dioxygenase is induced by pathogen attack and heavy metal stress activation through jasmonate signaling
J. Plant Physiol.
162
912-920
2005
Oryza sativa (Q9M5J1), Oryza sativa
brenda
Meisner, A.K.; Saffert, A.; Schreier, P.; Schoen, A.
Fatty acid alpha-dioxygenase from Pisum sativum temporal and spatial regulation during germination and plant development
J. Plant Physiol.
166
333-343
2009
Pisum sativum (Q5GQ66), Pisum sativum
brenda
Avila, C.A.; Arevalo-Soliz, L.M.; Lorence, A.; Goggin, F.L.
Expression of alpha-dioxygenase 1 in tomato and Arabidopsis contributes to plant defenses against aphids
Mol. Plant Microbe Interact.
26
977-986
2013
Solanum lycopersicum (Q69F00), Arabidopsis thaliana (Q9SGH6)
brenda
Gaquerel, E.; Steppuhn, A.; Baldwin, I.
Nicotiana attenuata alpha-dioxygenase1 through its production of 2-hydroxylinolenic acid is required for intact plant defense expression against attack from Manduca sexta larvae
New Phytol.
196
574-585
2012
Nicotiana attenuata
brenda
De Leon, I.; Sanz, A.; Hamberg, M.; Castresana, C.
Involvement of the Arabidopsis alpha-DOX1 fatty acid dioxygenase in protection against oxidative stress and cell death
Plant J.
29
61-72
2002
Arabidopsis thaliana (Q9SGH6)
brenda
Hong, C.E.; Ha, Y.I.; Choi, H.; Moon, J.Y.; Lee, J.; Shin, A.Y.; Park, C.J.; Yoon, G.M.; Kwon, S.Y.; Jo, I.H.; Park, J.M.
Silencing of an alpha-dioxygenase gene, Ca-DOX, retards growth and suppresses basal disease resistance responses in Capsicum annum
Plant Mol. Biol.
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Capsicum annuum
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Saffert, A.; Hartmann-Schreier, J.; Schoen, A.; Schreier, P.
A dual function alpha-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing alpha-oxidation of fatty acids in plants
Plant Physiol.
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Pisum sativum
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Liu, W.; Wang, L.; Fabian, P.; Hayashi, Y.; McGinley, C.; van der Donk, W.; Kulmacz, R.
Arabidopsisxa0thaliana fatty acid alpha-dioxygenase-1 evaluation ofxa0substrates, inhibitors andxa0amino-terminal function
Plant Physiol. Biochem.
44
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Arabidopsis thaliana (Q9SGH6)
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Zhu, G.; Koszelak-Rosenblum, M.; Malkowski, M.G.
Crystal structures of alpha-dioxygenase from Oryza sativa insights into substrate binding and activation by hydrogen peroxide
Protein Sci.
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Oryza sativa (Q9M5J1)
brenda
Akakabe, Y.; Matsui, K.; Kajiwara, T.
Enantioselective alpha-hydroperoxylation of long-chain fatty acids with crude enzyme of marine green alga Ulva pertusa
Tetrahedron Lett.
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Ulva pertusa
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brenda
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