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Information on EC 4.2.1.121 - colneleate synthase and Organism(s) Solanum tuberosum and UniProt Accession Q9AVQ1
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4.2.1.121 colneleate synthaseIUBMB Comments
A heme-thiolate protein (P-450) . It catalyses the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid . 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.
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Word Map
- 4.2.1.121
- hydroperoxide
-
linoleic
- oxylipins
-
allene
-
13-hydroperoxide
-
colneleic
-
9-hydroperoxides
- epoxyalcohols
- flax
-
phytophthora
- 9-lipoxygenase
- infestans
-
13-hpot
- ranunculus
- cyp74c
-
selaginella
-
9-hydroperoxy
-
spikemoss
The taxonomic range for the selected organisms is: Solanum tuberosum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
divinyl ether synthase, ledes, ntdes1, 9-des, cyp74d, dve synthase, 9-divinyl ether synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
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
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate = (8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoate + H2O
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
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
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
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
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
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
(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
the corresponding 13-hydroperoxide is not accepted as substrate
i.e. colnelenic acid
-
?
(9S)-hydroperoxylinoleic acid + H2O
?
-
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
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid + H2O
colneleic acid
-
-
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
-
-
i.e. colneleic 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
-
-
i.e. colnelenic acid
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid + H2O
colnelenic acid
-
-
i.e 9-[1'E,3'Z,6'Z-nonatrienyloxy]-8E-nonenoic acid
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
-
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
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
-
-
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
-
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
-
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
-
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
-
?
additional information
?
-
13-hydroperoxides are only poor substrates
-
-
?
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
?
-
-
the enzyme utilizes linoleic and alpha-linolenic acid 9-hydroperoxides as substrates, but is inactive towards 13-hydroperoxides
-
-
?
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
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
(8E)-9-[(1E,3Z)-nona-1,3-dien-1-yloxy]non-8-enoic acid + H2O
-
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
-
-
i.e. colneleate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0261
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
pH 6.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
accumulation of divinyl ether synthase transcripts both upon infiltration of potato leaves with Pseudomonas syringae and after infection with Phytophthora infestans
-
preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
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). DES_SOLTU
478
0
54114
Swiss-Prot
other Location (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
infiltration with Pseudomonas syringae pv. maculicola leads to high expression of 9-DES after 612 h
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hamberg, M.
Hidden stereospecificity in the biosynthesis of divinyl ether fatty acids
FEBS J.
272
736-743
2005
Solanum tuberosum
Stumpe, M.; Kandzia, R.; Gobel, C.; Rosahl, S.; Feussner, I.
A pathogen-inducible divinyl ether synthase (CYP74D) from elicitor-treated potato suspension cells
FEBS Lett.
507
371-376
2001
Solanum tuberosum (Q9AVQ1), Solanum tuberosum
Gbel, C.; Feussner, I.; Schmidt, A.; Scheel, D.; Sanchez-Serrano, J.; Hamberg, M.; Rosahl, S.
Oxylipin profiling reveals the preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
J. Biol. Chem.
276
6267-6273
2001
Solanum tuberosum
Crombie, L.; Morgan, D.O.; Smith, E.H.
The enzymic formation of colneleic acid, a divinyl ether fatty acid: experiments with [(9S)-18O2]hydroperoxyoctadeca-(10E),(12Z)-dienoic acid
J. Chem. Soc. Chem. Commun.
1987
502-503
1987
Solanum tuberosum
-
Crombie, L.; Morgan, D.O.; Smith, E.H.
An isotopic study (2H and 18O) of the enzymic conversion of linoleic acid into colneleic acid with carbon chain fracture: the origin of shorter chain aldehydes
J. Chem. Soc. Perkin Trans. I
1991
567-575
1991
Solanum tuberosum
-
Fahlstadius, P.; Hamberg, M.
Stereospecific removal of the pro-R hydrogen at C-8 of (9S)-hydroperoxyoctadecadienoic acid in the biosynthesis of colneleic acid
J. Chem. Soc. Perkin Trans.
1990
2027-2030
1990
Solanum tuberosum, Solanum tuberosum Bintje
-
Stumpe, M.; Feussner, I.
Formation of oxylipins by CYP74 enzymes
Phytochem. Rev.
5
347-357
2006
Solanum tuberosum (Q9AVQ1)
-
Eschen-Lippold, L.; Rothe, G.; Stumpe, M.; Goebel, C.; Feussner, I.; Rosahl, S.
Reduction of divinyl ether-containing polyunsaturated fatty acids in transgenic potato plants
Phytochemistry
68
797-801
2007
Solanum tuberosum
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