Information on EC 4.2.1.121 - colneleate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Solanaceae

EC NUMBER
COMMENTARY
4.2.1.121
-
RECOMMENDED NAME
GeneOntology No.
colneleate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
show the reaction diagram
-
-
-
-
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
show the reaction diagram
the oxygen inserted enzymically between carbons 9- and 10- of the C-18 chain in forming colneleic acid originates from 18O2 gas via the hydroperoxide group of linoleic acid. A mechanism is proposed
-
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
show the reaction diagram
intervention of an epoxycarbonium ion intermediate. A mechanism is proposed
-
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
show the reaction diagram
selective removal of the pro-R hydrogen at C-8 in the biosynthesis of colneleic acid
-
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
show the reaction diagram
selective removal of the pro-R hydrogen at C-8 in the biosynthesis of colneleic acid
Solanum tuberosum Bintje
-
-
PATHWAY
KEGG Link
MetaCyc Link
divinyl ether biosynthesis I
-
SYSTEMATIC NAME
IUBMB Comments
(8E)-9-[(1E,3E)-nona-1,3-dien-1-yloxy]non-8-enoate synthase
A heme-thiolate protein (P450) [2]. It catalyses the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid [4]. It forms also (8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid (i.e. colnelenate) from (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate. The corresponding 13-hydroperoxides are poor substrates [1,3]. The divinyl ethers colneleate and colnelenate have antimicrobial activity.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9-DES
Q9AVQ1
-
9-divinyl ether synthase
-
-
9-divinyl ether synthase
-
-
9-divinyl ether synthase
Q9AVQ1
-
CYP74 cytochrome P-450
Q9FPM6
-
CYP74D
Q9AVQ1
-
CYP74D1
Q9FPM6
-
DES
Q9AVQ1
-
divinyl ether synthase
-
-
divinyl ether synthase
Q9AVQ1
-
DVE synthase
-
-
LeDES
Q9FPM6
-
NtDES1
Q8W2N5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
LeDES is a single copy gene located on the distal half of the long arm of chromosome one; cv. Castlemart
UniProt
Manually annotated by BRENDA team
cv. Desiree
-
-
Manually annotated by BRENDA team
var. Bintje
-
-
Manually annotated by BRENDA team
Solanum tuberosum Bintje
Bintje
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
physiological function
Q8W2N5
9-lipoxygenase and divinyl ether synthase act together and form divinyl ethers in response to pathogen attack
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9S)-hydroperoxylinoleic acid + H2O
colneleic acid
show the reaction diagram
-
-
-
-
?
(9S)-hydroperoxylinoleic acid + H2O
?
show the reaction diagram
-
potato divinyl ether synthase stereospecifically utilizes (9S)-hydroperoxylinoleic acid
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-
-
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9AVQ1, -
-
i.e. colneleate, the fatty acid derivative colneleate functions as a plant antimicrobial compound
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-
intervention of an epoxycarbonium ion intermediate. A mechanism is proposed
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9FPM6, -
poorly active against the the corresponding 13-hydroperoxide
i.e. colneleate, characterization of the product
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-
selective removal of the pro-R hydrogen at C-8 in the biosynthesis of colneleic acid
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-
selective removal of the pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. Generation of colneleic acid from the (8R)-deuterated (9S)-hydroperoxide is accompanied by loss of most of the deuterium label (retention, 8%)
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-, Q8W2N5
the corresponding 13-hydroperoxide is a poor substrate
i.e. colneleate, characterization of the product
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9AVQ1, -
the corresponding 13-hydroperoxide is not accepted as substrate
i.e. colneleate, characterization of the product
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Solanum tuberosum Bintje
-
-, selective removal of the pro-R hydrogen at C-8 in the biosynthesis of colneleic acid
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid + H2O
colneleic acid
show the reaction diagram
-
-
i.e. 9-[1'E,3'Z-nonadienyloxy]-8E-nonenoic acid
-
?
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate + H2O
9-[1'(E),3'(Z)-nonadienyloxy]-8(E)-nonenoic acid
show the reaction diagram
-
-
i.e. colneleic acid
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
(8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9FPM6, -
poorly active against the the corresponding 13-hydroperoxide
i.e. colnelenate
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
(8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-, Q8W2N5
the corresponding 13-hydroperoxide is a poor substrate
i.e. colnelenate
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
(8E)-9-[(1E,3Z,6Z)-nona-1,3,6-trien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9AVQ1, -
the corresponding 13-hydroperoxide is not accepted as substrate
i.e. colnelenic acid
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid + H2O
9-[1'(E),3'(Z),6'(Z)-nonatrienyloxy]-8(E)-nonenoic acid
show the reaction diagram
-
-
i.e. colnelenic acid
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid + H2O
colnelenic acid
show the reaction diagram
-
-
i.e 9-[1'E,3'Z,6'Z-nonatrienyloxy]-8E-nonenoic acid
-
?
additional information
?
-
-
irrespective of which hydroperoxide regioisomer serves as the substrate, divinyl ether synthases abstracting the pro-R hydrogen generate divinyl ethers having an (E)-vinyl ether double bond, whereas enzymes abstracting the pro-S hydrogen produce divinyl ethers having a (Z)-vinyl ether double bond
-
-
-
additional information
?
-
-
13-hydroperoxides are only poor substrates
-
-
-
additional information
?
-
-
the enzyme utilizes linoleic and alpha-linolenic acid 9-hydroperoxides as substrates, but is inactive towards 13-hydroperoxides
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
-
-
i.e. colneleate
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Q9AVQ1, -
-
i.e. colneleate, the fatty acid derivative colneleate functions as a plant antimicrobial compound
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
show the reaction diagram
Solanum tuberosum Bintje
-
-
i.e. colneleate
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cytochrome P-450
Q9FPM6
the enzyme has spectral properties of cytochrome P-450
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0174
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
pH 6.5
0.067
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Q9FPM6
pH 7.0, 25C
0.0261
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
pH 6.5
0.048
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Q9FPM6
pH 7.0, 25C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
890
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Q9FPM6
pH 7.0, 25C
500
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Q9FPM6
pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13280
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Q9FPM6
pH 7.0, 25C
293316
10420
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Q9FPM6
pH 7.0, 25C
293317
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
Manually annotated by BRENDA team
-
accumulation of divinyl ether synthase transcripts both upon infiltration of potato leaves with Pseudomonas syringae and after infection with Phytophthora infestans
Manually annotated by BRENDA team
-
present in roots of green-house-grown potato plants
Manually annotated by BRENDA team
Q9FPM6
LeDES transcripts are most abundant in roots. A low level of LeDES mRNA is observed in stem tissue, but no accumulation is detected in flower buds, petioles, cotyledons, or leaves. Extracts from roots of young plants, but not extracts from stem or leaf tissue, catalyze efficient formation of colneleate from the hydroperoxide precursor
Manually annotated by BRENDA team
Q9FPM6
LeDES transcripts are most abundant in roots. A low level of LeDES mRNA is observed in stem tissue, but no accumulation is detected in flower buds, petioles, cotyledons, or leaves. Extracts from roots of young plants, but not extracts from stem or leaf tissue, catalyze efficient formation of colneleate from the hydroperoxide precursor
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q9FPM6
x * 55254, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant glutathione S-transferase fusion protein
Q8W2N5
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli as a glutathione S-transferase fusion protein
Q8W2N5
expression in Escherichia coli
Q9FPM6
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DES1 gene expression is not detectable in healthy or wounded stems, leaves and roots of tobacco plants
-
ethylene and methyl jasmonate positively stimulate the transcription of DES1
-
infiltration with Pseudomonas syringae pv. maculicola leads to high expression of 9-DES after 612 h
-