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Information on EC 5.3.99.6 - allene-oxide cyclase
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5.3.99.6 allene-oxide cyclaseIUBMB Comments
Allene oxides formed by the action of EC 4.2.1.92 hydroperoxide dehydratase, are converted into cyclopentenone derivatives.
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Word Map
- 5.3.99.6
-
jasmonic
-
12-oxo-phytodienoic
- oxylipins
-
octadecanoids
-
13s-lipoxygenase
-
phytodienoic
-
ja-deficient
-
hebiba
- 12-opda
-
ja-ile
- agriculture
-
12-oxo-pda
-
tulipae
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
allene oxide cyclase, osaoc, pnaoc, aaaoc, allene-oxide cyclase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Allene oxide cyclase
AOC
AOC1
AOC2
AOC3
Cyclase, allene oxide
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-
-
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EC 5.3.99.1
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-
formerly
-
Allene oxide cyclase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate
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-
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(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate
reaction is promoted by anchimeric assistance through a conserved Glu residue. The transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable pi-pi interactions with aromatic residues in the cavity
-
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate
the transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable pi-pi interactions with aromatic residues in the cavity. Stereoselectivity results from steric restrictions to the necessary substrate isomerizations imposed by the protein environment
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate = (15Z)-12-oxophyto-10,15-dienoate
catalytic mechanism of AOC isozymes: (1) a resting state of the apo enzyme with a closed conformation, (2) a first shallow binding mode, followed by (3) a tight binding of the substrate accompanied by conformational changes in the binding pocket, and (4) initiation of the catalytic cycle by opening of the epoxide ring. Cyclization of the allene oxide seems to be initiated by one particular Glu residue in the active site of AOC that leads to an opening of the epoxy ring, conformational changes, and a concerted pericyclic ring closure
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
intramolecular oxidoreduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(9Z)-(13S)-12,13-Epoxyoctadeca-9,11,15-trienoate isomerase (cyclizing)
Allene oxides formed by the action of EC 4.2.1.92 hydroperoxide dehydratase, are converted into cyclopentenone derivatives.
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CAS REGISTRY NUMBER
COMMENTARY
118390-59-3
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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
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
(12,13S)-epoxy-(9Z,11E,15Z)-octadecatrienoic acid
12-oxo-phytodienoic acid
-
-
-
-
?
(12S)-hydroperoxy eicosatetraenoic acid
11-oxoprostatrienoic acid
20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid
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-
?
(12Z)-9,10-epoxy-10,12-octadecadienoic acid
rac-cis-10-oxo-11-phytoenoic acid
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CYP74C3 catalyzes the synthesis, hydrolysis and cyclization of allene oxide
in addition, formation of some alpha-ketol
-
?
(5Z,8Z,10Z)-10-[3-[(2Z)-oct-2-en-1-yl]oxiran-2-ylidene]deca-5,8-dienoic acid
(5Z,14Z)-11-oxoprosta-5,9,14-trien-1-oic acid
-
substrate for isoenzyme PpAOC2
-
-
?
(9Z,11E)-11-[(3S)-3-[(2Z)-pent-2-en-1-yl]oxiran-2-ylidene]undec-9-enoic acid
8-[(1R,5S)-4-oxo-5-[(2Z)-pent-2-en-1-yl]cyclopent-2-en-1-yl]octanoic acid
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-
i.e. cis-(+)-OPDA
-
?
(9Z,13S,15Z)-12,13-epoxy-9,11,15-octadecatrienoic acid
(9S,13S)-12-oxo-phytodienoic acid
-
-
-
-
?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
-
?
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid
(9S,13S)-12-oxo-(10,15Z)-phytodienoic acid
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-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
Q8L6H4
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-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
Q8L6H4
enzyme catalyzes a late step in the jasmonic acid biosynthetic pathway
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?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
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-
-
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?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
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-
-
?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
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-
-
?
13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
cis-(+)-12-oxophytodienoic acid
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93.9% of cis-(+)-12-oxophytodienoic acid
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?
13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
cis-(+)-12-oxophytodienoic acid
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94.1% of cis-(+)-12-oxophytodienoic acid
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?
13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
cis-(+)-12-oxophytodienoic acid
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isoform AOC1, 91.3% of cis-(+)-12-oxophytodienoic acid
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?
13(S)-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid
cis-(+)-12-oxophytodienoic acid
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isoforms AOC2, 93.6%of cis-(+)-12-oxophytodienoic acid
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?
additional information
?
-
all Arabidopsis allene oxide cyclase isoforms may contribute to jasmonate biosynthesis
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-
?
additional information
?
-
all Arabidopsis allene oxide cyclase isoforms may contribute to jasmonate biosynthesis
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-
?
additional information
?
-
all Arabidopsis allene oxide cyclase isoforms may contribute to jasmonate biosynthesis
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-
?
additional information
?
-
all Arabidopsis allene oxide cyclase isoforms may contribute to jasmonate biosynthesis
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-
?
additional information
?
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all Arabidopsis allene oxide cyclase isoforms may contribute to jasmonate biosynthesis
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-
?
additional information
?
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allene oxides formed by the action of EC 4.2.1.92 are converted into cyclopentanone derivatives
-
-
?
additional information
?
-
-
enzyme of a branch leading specifically from (13S)-hydroperoxy-(9Z,11E,15Z)-octatrienoic acid to 12-oxo-phytodienoic acid, the precursor of jasmonic acid
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?
additional information
?
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role for jasmonic acid in the transfer of the assimilate to seeds
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?
additional information
?
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enzyme plays an essential role in formation of jasmonic acid induced by theobroxide
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?
additional information
?
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
additional information
?
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
additional information
?
-
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
additional information
?
-
substrate specificity of isozyme AOC2, overview
-
-
?
additional information
?
-
substrate specificity of isozyme AOC2, overview
-
-
?
additional information
?
-
-
substrate specificity of isozyme AOC2, overview
-
-
?
additional information
?
-
substrate specificity of wild-type and mutant isozymes AOC1, overview. The substrate dihydro analogue cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid does not cyclize in the presence of PpAOC1, but when bound to the enzyme, it undergoes isomerization into the corresponding trans-epoxide. AOc1 shows no activity with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid
-
-
?
additional information
?
-
substrate specificity of wild-type and mutant isozymes AOC1, overview. The substrate dihydro analogue cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid does not cyclize in the presence of PpAOC1, but when bound to the enzyme, it undergoes isomerization into the corresponding trans-epoxide. AOc1 shows no activity with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant isozymes AOC1, overview. The substrate dihydro analogue cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid does not cyclize in the presence of PpAOC1, but when bound to the enzyme, it undergoes isomerization into the corresponding trans-epoxide. AOc1 shows no activity with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid
-
-
?
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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
(9Z,13S,15Z)-12,13-epoxy-9,11,15-octadecatrienoic acid
(9S,13S)-12-oxo-phytodienoic acid
-
-
-
-
?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
Q8L6H4
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
Q8L6H4
enzyme catalyzes a late step in the jasmonic acid biosynthetic pathway
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate
(15Z)-12-oxophyto-10,15-dienoate
-
-
-
-
?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
-
-
-
?
(9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate
(9S,13S,15Z)-12-oxophyto-10,15-dienoate
-
-
-
?
additional information
?
-
-
allene oxides formed by the action of EC 4.2.1.92 are converted into cyclopentanone derivatives
-
-
?
additional information
?
-
-
enzyme of a branch leading specifically from (13S)-hydroperoxy-(9Z,11E,15Z)-octatrienoic acid to 12-oxo-phytodienoic acid, the precursor of jasmonic acid
-
-
?
additional information
?
-
-
role for jasmonic acid in the transfer of the assimilate to seeds
-
-
?
additional information
?
-
-
enzyme plays an essential role in formation of jasmonic acid induced by theobroxide
-
-
?
additional information
?
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
additional information
?
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
additional information
?
-
-
the plant contains two isozymes, PpAOC1 and PpAOC2, with different substrate specificities for C18- and C20-derived substrates, respectively. Comparison of complex structures of the C18 substrate analogue with in silico modeling of the C20 substrate analogue bound to the enzyme allows identification of the three major molecular determinants responsible for the different substrate specificities, i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
mRNA expression is induced by salt stress and low temperature, 300 mM NaCl, 4°C
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Do jasmonates play a role in arbuscular mycorrhiza-induced local bioprotection of Medicago truncatula against root rot disease caused by Aphanomyces euteiches?
Infections
Role of pathogen-induced volatiles in the Nicotiana tabacum-Golovinomyces cichoracearum interaction.
Infections
Stunted Growth Caused by Blast Disease in Rice Seedlings Is Associated with Changes in Phytohormone Signaling Pathways.
Starvation
The potassium-dependent transcriptome of Arabidopsis reveals a prominent role of jasmonic acid in nutrient signaling.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
jasmonic acid deficiency in AOC-interfering RNA plants does not influence resistance to Magnaporthe grisea or the pathogenesis-related gene expressions in these plants
additional information
Q8L6H4
jasmonic acid deficiency in AOC-interfering RNA plants does not influence resistance to Magnaporthe grisea or the pathogenesis-related gene expressions in these plants
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
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
induction of enzyme, lipoxygenase and allene oxide synthase, by treatment with theobroxide both under short day and long day conditions. Biphasic activation of enzyme by theobroxide, first level of activation together with elevated levels of jasmonic acid is observed within 30 min after treatment
-
-
brenda
isoform CYP74C3, a multifunctional enzyme synthesizing allene oxide and catalyzing its hydrolysis and cyclization
-
-
brenda
together with 13-lipoxygenase LOX H3 and allene oxide synthase, allene oxide cyclase protein accumulates upon wounding
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
allene oxide cyclase is present in epidermal, cortical and pith parenchymic cells showing the highest levels in vascular tissues surrounding cells
brenda
-
allene oxide cyclase is present in epidermal, cortical and pith parenchymic cells showing the highest levels in vascular tissues surrounding cells
brenda
-
allene oxide cyclase is present in epidermal, cortical and pith parenchymic cells showing the highest levels in vascular tissues surrounding cells
brenda
-
developing stolon, allene oxide cyclase and lipoxygenase are clearly detectable and levels do not change during development. Jasmonic acid treatment for 24 h increases protein levels of both enzymes. Both are present in the apex and along the stolon axis. Allene oxide cyclase is present in epidermal, cortical and pith parenchymic cells showing the highest levels in vascular tissues surrounding cells
brenda
-
allene oxide cyclase is present in epidermal, cortical and pith parenchymic cells showing the highest levels in vascular tissues surrounding cells
brenda
additional information
induction by jasmonates, octadecanoids and abscisic acid or during stress
brenda
additional information
-
ubiquitous expression, expression pattern analysis, overview
brenda
additional information
constitutive expression in all organs tested
brenda
additional information
-
constitutive expression in all organs tested
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
all enzymes of the lipoxygenase pathway differentially localize within chloroplasts. Allene oxide cyclase is weakly associated with the thylakoid membrane and also detected in the stroma
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
deletion mutants of AOC1 and AOC2 show reduced fertility, aberrant sporophyte morphology and interrupted sporogenesis
malfunction
Q8L6H4
two photomorphogenic mutants of rice, coleoptile photomorphogenesis 2 (cpm2) and hebiba, are defective in the gene encoding allene oxide cyclase, phenotypes, overview. Both mutants are more susceptible than wild-type to an incompatible strain of Magnaporthe oryzae in such a way that hyphal growth is enhanced in mutant tissues. Blast-induced accumulation of phytoalexins, especially that of the flavonoid sakuranetin, is severely impaired in cpm2 and hebiba
malfunction
-
12-oxophytodienoic acid-deficient rice allene oxide cyclase mutants show an increased tolerance to salt stress
malfunction
-
loss-of-function of isoform AOC3 renders plants more susceptible to nematode Meloidogyne javanica infection
metabolism
allene oxide cyclase is a key enzyme in jasmonates biosynthetic pathway
metabolism
allene oxide cyclase is the most important enzyme for the jasmonic acid biosynthesis
metabolism
-
isoforms AOC1 and AOC2 are key enzymes in the formation of jasmonic acid and its precursor (9S,13S)-12-oxo-phytodienoic acid
metabolism
-
key enzyme of the jasmonate biosynthetic pathway catalysing the formation of (9S,13S)-12-oxo-phytodienoic acid and establishes the stereochemical configuration of naturally occurring jasmonate. Spontaneous hydrolysis of the allene oxide also yields (9S,13S)-12-oxo-phytodienoic acid, although in its racemic form
metabolism
Q8L6H4
the enzyme is involved in the biosynthesis of jasmonic acid and related compounds
metabolism
the first specific step in the biosynthesis of the cyclopentanone class of oxylipins is catalyzed by allene oxide cyclase that forms cis(+)-12-oxo-phytodienoic acid. After reduction of the cyclopentenone by cis(+)-12-oxo-phytodienoic acid reductase isoform 3, the octanoic or hexanoic side chain is shortened by beta-oxidation cycles, pathway overview
physiological function
Q8L6H4
the rice allene oxide cyclase functions in defence against blast fungus Magnaporthe oryzae through the pathway of jasmonate production
physiological function
-
enzyme overexpression leads to an enhanced level of tolerance to salinity and increased jasmonic acid accumulation in wounded leaves
physiological function
-
the enzyme can regulate the synthesis of rice phenolic acids and thus allelopathic inhibition on barnyardgrass
physiological function
-
the enzyme is a signaling molecule regulating growth and the response to wounding in the liverwort Marchantia polymorpha
physiological function
-
the enzyme plays an important role in increasing the expression of transcription factors (MYB2 and ONAC045) and functional genes (DREB1F and LEA3) in transgenic rice under salt stress as well as improve stress tolerance through the accumulation of compatible solutes (proline and soluble sugar)
additional information
comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
additional information
comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
additional information
-
comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
additional information
-
contents of artemisinin, dihydroartemisinic acid and artemisinic acid, as well as jasmonate levels and expression levels of farnesyl diphosphate synthase, cytochrome P450 dependent hydroxylase, and double bond reductase 2, are increased significantly in AaAOC overexpression Artemisia annua plants
additional information
structural changes of the catalytic center lead to an open and closed conformation of PpAOC2. Comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
additional information
structural changes of the catalytic center lead to an open and closed conformation of PpAOC2. Comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
additional information
-
structural changes of the catalytic center lead to an open and closed conformation of PpAOC2. Comparison of active site structures of isozymes AOC1 and AOC2 and structure-function relationship, detailed overview
Show AA Sequence and Transmembrane Helices (825 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
recombinant protein, determined by SDS-PAGE and Western blot analysis
33000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
contains a putative chloroplast targeting sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of complexes with substrate 12,13-epoxy-9,11,15-octadecatrienoic acid and product 12-oxo-phytodienoic acid. Reaction is promoted by anchimeric assistance through a conserved Glu residue. The transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable pi-pi interactions with aromatic residues in the cavity
-
purified recombinant free isozyme AOC2, X-ray diffraction structure determination and analysis at 1.95 A resolution
purified recombinant isozyme AOC1, free or in complex with substrate analogue 12,13S-epoxy-9Z,15Z-octadecadienoic acid, X-ray diffraction structure determination and analysis at 1.35-2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C71A
97.7% of wild-type activity, 94.1% yield of cis-(+)-12-oxophytodienoic acid
C71S
97.1% of wild-type activity, 93.9% yield of cis-(+)-12-oxophytodienoic acid
C71Y
33.3% of wild-type activity, 67.4% yield of cis-(+)-12-oxophytodienoic acid
E23A
F43Y
90.4% of wild-type activity, 93.5% yield of cis-(+)-12-oxophytodienoic acid
F51A
128.4% of wild-type activity, 94.7% yield of cis-(+)-12-oxophytodienoic acid
F85A
54.7% of wild-type activity, 71.7% yield of cis-(+)-12-oxophytodienoic acid
F85L
79.6% of wild-type activity, 87.7% yield of cis-(+)-12-oxophytodienoic acid
K152A/E80A
the mutant shows strongly reduced activity compared to the wild type enzyme
K152A/E80A/L53S
the mutant shows strongly reduced activity compared to the wild type enzyme
L27R
101.3% of wild-type activity, 92.8% yield of cis-(+)-12-oxophytodienoic acid
L53S
the mutant shows strongly reduced activity compared to the wild type enzyme
N25L
38.6% of wild-type activity, 63.4% yield of cis-(+)-12-oxophytodienoic acid
N53L
248% of wild-type activity, 83.4% yield of cis-(+)-12-oxophytodienoic acid
P32V
61% of wild-type activity, 57.1% yield of cis-(+)-12-oxophytodienoic acid
S31A
75.8% of wild-type activity, 71.8% yield of cis-(+)-12-oxophytodienoic acid
S31A/N53L
93.6% of wild-type activity, 84.9% yield of cis-(+)-12-oxophytodienoic acid
V49F
130.4% of wild-type activity, 93.0% yield of cis-(+)-12-oxophytodienoic acid
F140V
site-directed mutagenesis, the mutant variant is active with the 13-hydroperoxy octadecatrienoic acid-derived allene oxide, but inactive with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid and (12S)-hydroperoxy eicosatetraenoic acid-derived allene oxide
F29I/F140V
site-directed mutagenesis, the mutant variant is active with the 13-hydroperoxy octadecatrienoic acid-derived allene oxide, but inactive with 20:4(n-6)-derived (12S)-hydroperoxy eicosatetraenoic acid and (12S)-hydroperoxy eicosatetraenoic acid-derived allene oxide
additional information
E23A
29% of wild-type activity, 57.6% yield of cis-(+)-12-oxophytodienoic acid
additional information
transgenic tobacco expressing Campotheca acuminata allene oxide cyclase displays higher chlorophyll content under salt stress than wild plants and is more resistant to low temperature. Expression of a 5'-truncated Campotheca acuminata allene oxide cyclase in Escherichia coli results in cells that can grow on agar plates containing 400 mM NaCl
additional information
-
transgenic tobacco expressing Campotheca acuminata allene oxide cyclase displays higher chlorophyll content under salt stress than wild plants and is more resistant to low temperature. Expression of a 5'-truncated Campotheca acuminata allene oxide cyclase in Escherichia coli results in cells that can grow on agar plates containing 400 mM NaCl
additional information
-
generation of a jasmonic acid-deficient rice line by suppression of allene oxide cyclase using RNAi. The level of resistance to Magnaporthe grisea infection is equal to wild-type and to a strain lacking 12-oxo-phytodienoic acid reductase
additional information
Q8L6H4
generation of a jasmonic acid-deficient rice line by suppression of allene oxide cyclase using RNAi. The level of resistance to Magnaporthe grisea infection is equal to wild-type and to a strain lacking 12-oxo-phytodienoic acid reductase
additional information
Q8L6H4
two photomorphogenic mutants of rice, coleoptile photomorphogenesis 2 (cpm2) and hebiba, are defective in the gene encoding allene oxide cyclase (OsAOC), map-based cloning and complementation assays, overview
additional information
-
two photomorphogenic mutants of rice, coleoptile photomorphogenesis 2 (cpm2) and hebiba, are defective in the gene encoding allene oxide cyclase (OsAOC), map-based cloning and complementation assays, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged OsAOC lacking the chloroplast transit peptide from Escherichia coli strain BL21 by glutathione affinity chromatography
Q8L6H4
recombinant N-terminally GST-tagged isozyme AOC1 from Escherichia coli by glutathione affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AOC1, expression as N-terminally GST-tagged enzyme in Escherichia coli
AOC2, expression as N-terminally GST-tagged enzyme in Escherichia coli
cloning of the promoter of AaAOC, the key gene of jasmonate biosynthetic pathway, expression analysis, AaAOC gene overexpression under control of the 35S promoter in Artemisia annua leading to an increase of 1.6 to 5.2fold in enzyme expression and 2 to 4.7fold increase in jasmonate levels, as well as to a significant increase of contents of artemisinin, dihydroartemisinic acid and artemisinic acid, expression analysis by RT-Q-PCR
-
gene OsAOC, OsAOC lacking the chloroplast transit peptide is amplified from cultivar Nihonmasari cDNA and expressed as GST-tagged enzyme in Escherichia coli strain BL21
Q8L6H4
generating of a jasmonic acid-deficient rice line with suppressed expression of the genes encoding AOC with resistance to Magnaporthe grisea by introduction into rice plants by Agrobacterium-mediated transformation, the expression of AOC is induced after jasmonic acid and wound treatment, AOC-interfering RNA plants show normal resistance to both an incompatible and a compatible race of Magnaporthe grisea
Q8L6H4
into the vector pGEM-T Easy for sequencing and subsequently into the vector pQE30 for expression in Escherichia coli M15 cells
into the vector pMD18-T and for expression in Escherichia coli BL21DE3 cells subsequently into the vector pET-30a
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by abscisic acid, methyl jasmonic acid, salicylic acid, cold stresses, polyethylene glycol, and salinity, particularly by high salinity (120 mM NaCl)
-
enzyme expression is induced by wounding and (15Z)-12-oxophyto-10,15-dienoate treatment
-
in wheat plants stressed with either NaCl or polyethylene glycerol , isoform AOC1 transcript abundance rises by, respectively, about 15 and 8fold
-
isoform AOC3 is highly induced during nematode Meloidogyne javanica infection
-
the enzyme expression under salicylic acid and wounding treatments is up-regulated. The mRNA expression of the enzyme can be induced by tea geometrids and tea green leafhoppers
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
biotechnology
-
constitutive overexpression of enzyme, 53fold increase of 12-oxo-phytodienoic acid methyl ester in stamen, 51fold increase of jasmonic acid in buds and 7.5fold increase in sepals. Increase in jasmonates and octadecanoids is accompanied by decreased levels of free lipid hydro(per)oxy compounds
agriculture
Q8L6H4
generation of a jasmonic acid-deficient rice line by suppression of allene oxide cyclase using RNAi. The level of resistance to Magnaporthe grisea infection is equal to wild-type and to a strain lacking 12-oxo-phytodienoic acid reductase
agriculture
transgenic tobacco expressing Campotheca acuminata allene oxide cyclase displays higher chlorophyll content under salt stress than wild plants and is more resistant to low temperature. Expression of a 5'-truncated Campotheca acuminata allene oxide cyclase in Escherichia coli results in cells that can grow on agar plates containing 400 mM NaCl
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hamberg, M.
Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of an allene oxide cyclase
Biochem. Biophys. Res. Commun.
156
543-550
1988
Zea mays
brenda
Simpson, T.D.; Gardner, H.W.
Allene oxide synthase and allene oxide cyclase, enzymes of the jasmonic acid pathway, localized in Glycine max tissues
Plant Physiol.
108
199-202
1995
Glycine max
brenda
Hamberg, M.; Fahlstadius, P.
Allene oxide cyclase: a new enzyme in plant metabolism
Arch. Biochem. Biophys.
276
518-526
1990
Allium cepa, Brassica oleracea, Cucumis sativus, Cucurbita pepo, Lactuca sativa, Solanum lycopersicum, Solanum melongena, Solanum tuberosum, Spinacia oleracea, Zea mays
brenda
Kong, F.; Abe, J.; Takahashi, K.; Matsuura, H.; Yoshihara, T.; Nabeta, K.
Allene oxide cyclase is essential for theobroxide-induced jasmonic acid biosynthesis in Pharbitis nil
Biochem. Biophys. Res. Commun.
336
1150-1156
2005
Ipomoea nil
brenda
Maucher, H.; Stenzel, I.; Miersch, O.; Stein, N.; Prasad, M.; Zierold, U.; Schweizer, P.; et al.
The allene oxide cyclase of barley (Hordeum vulgare L.) - cloning and organ-specific expression
Phytochemistry
65
801-811
2004
Hordeum vulgare (Q711R0), Hordeum vulgare
brenda
Miersch, O.; Weichert, H.; Stenzel, I.; Hause, B.; Maucher, H.; Feussner, I.; Wasternack, C.
Constitutive overexpression of allene oxide cyclase in tomato (Lycopersicon esculentum cv. Lukullus) elevates levels of some jasmonates and octadecanoids in flower organs but not in leaves
Phytochemistry
65
847-856
2004
Solanum lycopersicum
brenda
Farmaki, T.; Sanmartin, M.; Jimenez, P.; Paneque, M.; Sanz, C.; Vancanneyt, G.; Leon, J.; Sanchez-Serrano, J.
Differential distribution of the lipoxygenase pathway
J. Exp. Bot.
58
555-568
2007
Solanum tuberosum (Q8H1X5), Solanum tuberosum
brenda
Cenzano, A.; Abdala, G.; Hause, B.
Cytochemical immuno-localization of allene oxide cyclase, a jasmonic acid biosynthetic enzyme, in developing potato stolons
J. Plant Physiol.
164
1449-1456
2007
Solanum tuberosum
brenda
Hofmann, E.; Zerbe, P.; Schaller, F.
The crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction
Plant Cell
18
3201-3217
2006
Arabidopsis thaliana
brenda
Yara, A.; Yaeno, T.; Hasegawa, M.; Seto, H.; Seo, S.; Kusumi, K.; Iba, K.
Resistance to Magnaporthe grisea in transgenic rice with suppressed expression of genes encoding allene oxide cyclase and phytodienoic acid reductase
Biochem. Biophys. Res. Commun.
376
460-465
2008
Oryza sativa, Oryza sativa (Q8L6H4)
brenda
Pi, Y.; Liao, Z.; Jiang, K.; Huang, B.; Deng, Z.; Zhao, D.; Zeng, H.; Sun, X.; Tang, K.
Molecular cloning, characterization and expression of a jasmonate biosynthetic pathway gene encoding allene oxide cyclase from Camptotheca acuminata
Biosci. Rep.
28
349-355
2008
Camptotheca acuminata (A9UKW1), Camptotheca acuminata
brenda
Grechkin, A.N.; Mukhtarova, L.S.; Latypova, L.R.; Gogolev, Y.; Toporkova, Y.Y.; Hamberg, M.
Tomato CYP74C3 is a multifunctional enzyme not only synthesizing allene oxide but also catalyzing its hydrolysis and cyclization
ChemBioChem
9
2498-2505
2008
Solanum lycopersicum
brenda
Schaller, F.; Zerbe, P.; Reinbothe, S.; Reinbothe, C.; Hofmann, E.; Pollmann, S.
The allene oxide cyclase family of Arabidopsis thaliana: localization and cyclization
FEBS J.
275
2428-2441
2008
Arabidopsis thaliana (Q93ZC5), Arabidopsis thaliana (Q9LS01), Arabidopsis thaliana (Q9LS02), Arabidopsis thaliana (Q9LS03), Arabidopsis thaliana
brenda
Pi, Y.; Jiang, K.; Cao, Y.; Wang, Q.; Huang, Z.; Li, L.; Hu, L.; Li, W.; Sun, X.; Tang, K.
Allene oxide cyclase from Camptotheca acuminata improves tolerance against low temperature and salt stress in tobacco and bacteria
Mol. Biotechnol.
41
115-122
2009
Camptotheca acuminata (A9UKW1), Camptotheca acuminata
brenda
Liu, B.; Wang, W.; Gao, J.; Chen, F.; Wang, S.; Xu, Y.; Tang, L.; Jia, Y.
Molecular cloning and characterization of a jasmonate biosynthetic pathway gene for allene oxide cyclase from Jatropha curcas
Acta Physiol. Plant.
32
531-539
2010
Jatropha curcas (D2D954)
-
brenda
Kong, F.J.; Li, Y.; Abe, J.; Liu, B.; Schaller, F.; Piotrowski, M.; Otagaki, S.; Takahashi, K.; Matsuura, H.; Yoshihara, T.; Nabeta, K.
Expression of allene oxide cyclase from Pharbitis nil upon theobroxide treatment
Biosci. Biotechnol. Biochem.
73
1007-1013
2009
Ipomoea nil (Q2PP43), Ipomoea nil
brenda
Cho, K.B.; Lai, W.; Hamberg, M.; Raman, C.S.; Shaik, S.
The reaction mechanism of allene oxide synthase: interplay of theoretical QM/MM calculations and experimental investigations
Arch. Biochem. Biophys.
507
14-25
2011
Arabidopsis thaliana
brenda
Stumpe, M.; Goebel, C.; Faltin, B.; Beike, A.K.; Hause, B.; Himmelsbach, K.; Bode, J.; Kramell, R.; Wasternack, C.; Frank, W.; Reski, R.; Feussner, I.
The moss Physcomitrella patens contains cyclopentenones but no jasmonates: mutations in allene oxide cyclase lead to reduced fertility and altered sporophyte morphology
New Phytol.
188
740-749
2010
Physcomitrium patens
brenda
Hashimoto, T.; Takahashi, K.; Sato, M.; Bandara, P.; Nabeta, K.
Cloning and characterization of an allene oxide cyclase, PpAOC3, in Physcomitrella patens
Plant Growth Regul.
65
239
2011
Physcomitrium patens
-
brenda
Lu, X.; Lin, X.; Shen, Q.; Zhang, F.; Wang, Y.; Chen, Y.; Wang, T.; Wu, S.; Tang, K.
Characterization of the jasmonate biosynthetic gene allene oxide cyclase in Artemisia annua L., source of the antimalarial drug artemisinin
Plant Mol. Biol. Rep.
29
489-497
2011
Artemisia annua
-
brenda
Riemann, M.; Haga, K.; Shimizu, T.; Okada, K.; Ando, S.; Mochizuki, S.; Nishizawa, Y.; Yamanouchi, U.; Nick, P.; Yano, M.; Minami, E.; Takano, M.; Yamane, H.; Iino, M.
Identification of rice allene oxide cyclase mutants and the function of jasmonate for defence against Magnaporthe oryzae
Plant J.
74
226-238
2013
Oryza sativa (Q8L6H4), Oryza sativa
brenda
Neumann, P.; Brodhun, F.; Sauer, K.; Herrfurth, C.; Hamberg, M.; Brinkmann, J.; Scholz, J.; Dickmanns, A.; Feussner, I.; Ficner, R.
Crystal structures of Physcomitrella patens AOC1 and AOC2: insights into the enzyme mechanism and differences in substrate specificity
Plant Physiol.
160
1251-1266
2012
Physcomitrium patens (Q8GS38), Physcomitrium patens (Q8H0N6), Physcomitrium patens
brenda
Lu, X.; Zhang, F.; Shen, Q.; Jiang, W.; Pan, Q.; Lv, Z.; Yan, T.; Fu, X.; Wang, Y.; Qian, H.; Tang, K.
Overexpression of allene oxide cyclase improves the biosynthesis of artemisinin in Artemisia annua L
PLoS ONE
9
e91741
2014
Artemisia annua
brenda
Wang, M.; Ma, Q.; Han, B.; Li, X.
Molecular cloning and expression of a jasmonate biosynthetic gene allene oxide cyclase from Camellia sinensis
Can. J. Plant Sci.
96
109-116
2016
Camellia sinensis (F1DRC0)
-
brenda
Naor, N.; Gurung, F.; Ozalvo, R.; Bucki, P.; Sanadhya, P.; Miyara, S.
Tight regulation of allene oxide synthase (AOS) and allene oxide cyclase-3 (AOC3) promote Arabidopsis susceptibility to the root-knot nematode Meloidogyne javanica
Eur. J. Plant Pathol.
150
149-165
2018
Arabidopsis thaliana
-
brenda
Liu, H.H.; Wang, Y.G.; Wang, S.P.; Li, H.J.
Cloning and characterization of peanut allene oxide cyclase gene involved in salt-stressed responses
Genet. Mol. Res.
14
2331-2340
2015
Arachis hypogaea
brenda
Hazman, M.; Hause, B.; Eiche, E.; Nick, P.; Riemann, M.
Increased tolerance to salt stress in OPDA-deficient rice allene oxide cyclase mutants is linked to an increased ROS-scavenging activity
J. Exp. Bot.
66
3339-3352
2015
Oryza sativa
brenda
Wang, L.; Zhu, Y.; Tong, X.; Hu, W.; Cai, C.; Guo, W.
Molecular cloning and characterization of an allene oxide cyclase gene associated with fiber strength in cotton
J. Integr. Agric.
13
2113-2121
2014
Gossypium barbadense, Gossypium raimondii, Gossypium herbaceum, Gossypium hirsutum (A0A075C530)
-
brenda
Yamamoto, Y.; Ohshika, J.; Takahashi, T.; Ishizaki, K.; Kohchi, T.; Matusuura, H.; Takahashi, K.
Functional analysis of allene oxide cyclase, MpAOC, in the liverwort Marchantia polymorpha
Phytochemistry
116
48-56
2015
Marchantia polymorpha
brenda
Fang, C.; Yu, Y.; Chen, W.; Jian, X.; Wang, Q.; Zheng, H.; Lin, W.
Role of allene oxide cyclase in the regulation of rice phenolic acids synthesis and allelopathic inhibition on barnyardgrass
Plant Growth Regul.
79
265-273
2016
Oryza sativa
-
brenda
Zhao, Y.; Dong, W.; Zhang, N.; Ai, X.; Wang, M.; Huang, Z.; Xiao, L.; Xia, G.
A wheat allene oxide cyclase gene enhances salinity tolerance via jasmonate signaling
Plant Physiol.
164
1068-1076
2014
Triticum aestivum
brenda
Koeduka, T.; Ishizaki, K.; Mwenda, C.M.; Hori, K.; Sasaki-Sekimoto, Y.; Ohta, H.; Kohchi, T.; Matsui, K.
Biochemical characterization of allene oxide synthases from the liverwort Marchantia polymorpha and green microalgae Klebsormidium flaccidum provides insight into the evolutionary divergence of the plant CYP74 family
Planta
242
1175-1186
2015
Solanum lycopersicum
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otto, m.; naumann, c.; brandt, w.; wasternack, c.; hause, b.
activity regulation by heteromerization of Arabidopsis allene oxide cyclase family members
Plants (Basel)
5
pii: E3
2016
Arabidopsis thaliana (Q9LS02), Arabidopsis thaliana
brenda
Zdyb, A.; Salgado, M.G.; Demchenko, K.N.; Brenner, W.G.; Plaszczyca, M.; Stumpe, M.; Herrfurth, C.; Feussner, I.; Pawlowski, K.
Allene oxide synthase, allene oxide cyclase and jasmonic acid levels in Lotus japonicus nodules
PLoS ONE
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e0190884
2018
Lotus japonicus
brenda
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