Information on EC 4.2.1.121 - colneleate synthase

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The expected taxonomic range for this enzyme is: Solanaceae

EC NUMBER
COMMENTARY hide
4.2.1.121
-
RECOMMENDED NAME
GeneOntology No.
colneleate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
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
PATHWAY
BRENDA Link
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 (P-450) [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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bintje
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
physiological function
9-lipoxygenase and divinyl ether synthase act together and form divinyl ethers in response to pathogen attack
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9S)-hydroperoxylinoleic acid + H2O
?
show the reaction diagram
-
potato divinyl ether synthase stereospecifically utilizes (9S)-hydroperoxylinoleic acid
-
-
?
(9S)-hydroperoxylinoleic acid + H2O
colneleic acid
show the reaction diagram
-
-
-
-
?
(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
(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
(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
(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
(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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P-450
the enzyme has spectral properties of cytochrome P-450
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0174 - 0.067
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
0.0261 - 0.048
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
890
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Solanum lycopersicum
Q9FPM6
pH 7.0, 25C
500
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Solanum lycopersicum
Q9FPM6
pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13280
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Solanum lycopersicum
Q9FPM6
pH 7.0, 25C
4439
10420
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Solanum lycopersicum
Q9FPM6
pH 7.0, 25C
7899
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
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
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55254, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant glutathione S-transferase fusion protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli as a glutathione S-transferase fusion protein
EXPRESSION
ORGANISM
UNIPROT
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
-