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Information on EC 4.2.1.121 - colneleate synthase and Organism(s) Solanum lycopersicum and UniProt Accession Q9FPM6

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.121 colneleate synthase
IUBMB 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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Solanum lycopersicum
UNIPROT: Q9FPM6
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Word Map
The taxonomic range for the selected organisms is: Solanum lycopersicum
The enzyme appears in selected viruses and cellular organisms
Synonyms
divinyl ether synthase, ledes, ntdes1, 9-des, 9-divinyl ether synthase, cyp74d, dve synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CYP74 cytochrome P-450
-
divinyl ether synthase
-
-
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) 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
poorly active against the the corresponding 13-hydroperoxide
i.e. colneleate, characterization of the product
-
?
(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
poorly active against the the corresponding 13-hydroperoxide
i.e. colnelenate
-
?
(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-octadecatrienoic acid + H2O
9-[1'(E),3'(Z),6'(Z)-nonatrienyloxy]-8(E)-nonenoic acid
show the reaction diagram
-
-
i.e. colnelenic acid
-
?
additional information
?
-
-
the enzyme utilizes linoleic and alpha-linolenic acid 9-hydroperoxides as substrates, but is inactive towards 13-hydroperoxides
-
-
?
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
0.067
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
pH 7.0, 25°C
0.048
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
890
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
pH 7.0, 25°C
500
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13280
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
pH 7.0, 25°C
10420
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
pH 7.0, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DES_SOLLC
478
0
54189
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55254
x * 55254, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 55254, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itoh, A.; Howe, G.A.
Molecular cloning of a divinyl ether synthase. Identification as a CYP74 cytochrome P-450
J. Biol. Chem.
276
3620-3627
2001
Solanum lycopersicum (Q9FPM6), Solanum lycopersicum
Manually annotated by BRENDA team
Grechkin, A.N.
Hydroperoxide lyase and divinyl ether synthase
Prostaglandins Other Lipid Mediat.
68-69
457-470
2002
Solanum lycopersicum, Solanum tuberosum
Manually annotated by BRENDA team