Any feedback?
Information on EC 1.14.14.58 - trimethyltridecatetraene synthase
for references in articles please use BRENDA:EC1.14.14.58Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.14.58 trimethyltridecatetraene synthaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C16 homoterpene in response to herbivore attack. In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59, dimethylnonatriene synthase).
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cyp82g1, cyp92c5, cyp92c6, dmnt/tmtt homoterpene synthase, at3g25180, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP82G1
CYP92C5
CYP92C6
DMNT/TMTT homoterpene synthase
TMTT synthase
CYP82G1
-
-
-
-
CYP92C5
-
-
-
-
CYP92C6
-
-
-
-
DMNT/TMTT homoterpene synthase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
-
-
-
-
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2 = (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
the exact mechanism of enzyme is not yet determined. It is possible that CYP82G1 may promote the direct transformation of (E,E)-geranyllinalool and (3R,6E)-nerolidol to (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene and (3E)-4,8-dimethylnona-1,3,7-triene, respectively, with the concomitant release of but-1-en-3-one. But it is also possible that a two-step conversion occurs that includes the formation of intermediate compounds C18 (E,E)-farnesylacetone (from (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene) and C13 (E)-geranylacetone (from (3E)-4,8-dimethylnona-1,3,7-triene). A C4-cleavage product (but-1-en-3-one) resulting from the breakdown of (E,E)-geranyllinalool or (E)-nerolidol is not observed, neither in vitro nor in vivo, and none of the previously proposed ketone intermediates, C18-farnesylacetone and C13-geranylacetone, are detected
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(6E,10E)-geranyllinalool,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase
A cytochrome P-450 (heme-thiolate) protein isolated from the plants Arabidopsis thaliana (thale cress) and Zea mays (maize). It forms this C16 homoterpene in response to herbivore attack. In vitro some variants of the enzyme also convert (3S,6E)-nerolidol to (3E)-4,8-dimethylnona-1,3,7-triene (see EC 1.14.14.59, dimethylnonatriene synthase).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
(E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
arabidiol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + ? + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
biosynthesis of the volatile organic compound (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
major substrate
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
B6ST66, B8A110
-
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
in vitro activity is 5.3fold higher than with (E,E)-geranyllinalool. (3E)-4,8-dimethylnona-1,3,7-triene is not emitted from Arabidopsis leaves (or only in negligible amounts according to our analysis) because of the absence of a prominent (E)-nerolidol synthase activity in this tissue
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
B6ST66, B8A110
-
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
B6ST66, B8A110
major substrate
-
-
?
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
-
-
-
?
(6E,10E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + [oxidized NADPH-hemoprotein reductase] + but-3-en-2-one + 2 H2O
B6ST66, B8A110
-
-
-
?
additional information
?
-
no activity with isophytol, (E)-geraniol, linalool, 3,7,11-trimethyl-3-dodecanol, (Z)-nerolidol. Less than 1% of the activity with (3S,6E)-nerolidol: (E,E,E)-geranylgeraniol, (E,E)-farnesylacetone, (E,E)-farnesol, (E)-geranylacetone. Construction of a protein model based on multiple mammalian P450 templates with closest sequence similarity. Subsequent molecular docking confirms a position of (E)-nerolidol and (E,E)-geranyllinalool in the active site cavity that allows the suggested oxidative bond cleavage reaction to proceed by a syn-elimination (beta-elimination) mechanism. In particular, the carbonyl oxygen of Thr313 in one of the substrate recognition sites appears to be essential for anchoring the substrates by forming a strong hydrogen bond with the hydroxyl group at C3. The model supported the observed differences in substrate specificities
-
-
?
additional information
?
-
cytochrome P450 monooxygenase with narrow substrate specificity for (E,E)-geranyllinalool and (E)-nerolidol. Mechanism follows oxidative bond cleavage of the alcohol substrate via syn-elimination of the polar head, together with an allylic C-5 hydrogen atom. No substrate: racemic linalool or (R)-(-)-linalool
-
-
?
additional information
?
-
-
linalool, (Z)-nerolidol, the primary terpene alcohols (E,E,E)-geranylgeraniol, (E,E)-farnesol, and (E)-geraniol, or fully saturated analogs of (E)-nerolidol and (E,E)-geranyllinalool (3,7,11-trimethyl-3-dodecanol, isophytol) are no functional substrates of the CYP82G1 enzyme
-
-
?
additional information
?
-
-
CYP705A1 cleaves the prenyl side chain of arabidiol to produce (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and a nonvolatile C19-ketone derivative
-
-
?
additional information
?
-
CYP705A1 cleaves the prenyl side chain of arabidiol to produce (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and a nonvolatile C19-ketone derivative
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
-
?
arabidiol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + ? + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
biosynthesis of the volatile organic compound (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene
-
-
?
(3S)-(E,E)-geranyllinalool + [reduced NADPH-hemoprotein reductase] + O2
(E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
B6ST66, B8A110
-
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
in vitro activity is 5.3fold higher than with (E,E)-geranyllinalool. (3E)-4,8-dimethylnona-1,3,7-triene is not emitted from Arabidopsis leaves (or only in negligible amounts according to our analysis) because of the absence of a prominent (E)-nerolidol synthase activity in this tissue
-
-
?
(3S,6E)-nerolidol + [reduced NADPH-hemoprotein reductase] + O2
(3E)-4,8-dimethylnona-1,3,7-triene + but-1-en-3-one + [oxidized NADPH-hemoprotein reductase] + 2 H2O
B6ST66, B8A110
-
-
-
?
additional information
?
-
-
linalool, (Z)-nerolidol, the primary terpene alcohols (E,E,E)-geranylgeraniol, (E,E)-farnesol, and (E)-geraniol, or fully saturated analogs of (E)-nerolidol and (E,E)-geranyllinalool (3,7,11-trimethyl-3-dodecanol, isophytol) are no functional substrates of the CYP82G1 enzyme
-
-
?
additional information
?
-
-
CYP705A1 cleaves the prenyl side chain of arabidiol to produce (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and a nonvolatile C19-ketone derivative
-
-
?
additional information
?
-
CYP705A1 cleaves the prenyl side chain of arabidiol to produce (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and a nonvolatile C19-ketone derivative
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00184
(3S)-(E)-nerolidol
pH not specified in the publication, temperature not specified in the publication
0.00268
(E,E)-geranyllinalool
pH and temperature not specified in the publication
0.00268
(3S)-(E,E)-geranyllinalool
pH not specified in the publication, temperature not specified in the publication
0.0056
(3S)-(E,E)-geranyllinalool
B6ST66, B8A110
pH and temperature not specified in the publication
0.0104
(3S)-(E,E)-geranyllinalool
B6ST66, B8A110
pH and temperature not specified in the publication
0.00184
(3S,6E)-nerolidol
pH and temperature not specified in the publication
0.0142
(3S,6E)-nerolidol
B6ST66, B8A110
pH and temperature not specified in the publication
0.0027
(6E,10E)-geranyllinalool
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
(3S)-(E)-nerolidol
pH not specified in the publication, temperature not specified in the publication
0.11
(3S)-(E,E)-geranyllinalool
pH not specified in the publication, temperature not specified in the publication
0.2
(3S,6E)-nerolidol
pH and temperature not specified in the publication
0.11
(6E,10E)-geranyllinalool
pH not specified in the publication, temperature not specified in the publication
0.11
(E,E)-geranyllinalool
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
109
(3S,6E)-nerolidol
pH and temperature not specified in the publication
50
(6E,10E)-geranyllinalool
pH not specified in the publication, temperature not specified in the publication
41
(E,E)-geranyllinalool
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme catalyzes reactions of EC 1.14.14.58 and of EC 1.14.14.59
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
highly coordinated herbivore-induced expression with geranyllinalool synthase in leaves depending on the F-box protein COI-1
brenda
highly coordinated herbivore-induced expression with geranyllinalool synthase in leaves
brenda
additional information
-
CYP705A1 clusters with the arabidiol synthase gene ABDS, and both genes are coexpressed constitutively in the root stele and meristematic tissue
brenda
additional information
CYP705A1 clusters with the arabidiol synthase gene ABDS, and both genes are coexpressed constitutively in the root stele and meristematic tissue
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
CYP705A1 is a member of the Brassicaceae-specific CYP705 family
evolution
B6ST66, B8A110
the DMNT biosynthetic pathway and both (DMNT and TMTT) monooxygenases are distinct from those previously characterized for (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT, synthesis in Arabidopsis thaliana, suggesting independent evolution of these enzymatic activities. The amino acid identity between the maize and Arabidopsis enzymes is below 30%
malfunction
CYP82G1 gene knockout plants do not produce (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene and their phenotype is complemented by the constitutive expression of CYP82G1
malfunction
the null mutant cyp82g1-1 is not impaired in root-specific DMNT biosynthesis, indicating that enzyme Cyp82g1 is not involved in the formation of DMNT in Arabidopsis thaliana roots
metabolism
enzyme CYP705A1 is involved in DMNT biosynthesis in Arabidopsis thaliana roots. The formation of (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, and (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene, TMTT, in leaf or flower tissues usually occurs by the oxidative breakdown of (E)-nerolidol or (E,E)-geranyl linalool. Arabidiol Is the precursor in DMNT biosynthesis in Arabidopsis thaliana roots, it can be degraded by CYP705A1 to a C19 ketone product (14-apo-arabidiol). Role of the DMNT biosynthetic pathway in resistance against Pythium irregulare
metabolism
B6ST66, B8A110
the C11 homoterpene (E)-4,8-dimethyl-1,3,7-nonatriene (DMNT) is formed by the oxidative degradation of (E)-nerolidol. (E,E)-4,8,12-Trimethyltrideca-1,3,7,11-tetraene (TMTT) is produced via oxidative degradation of (E,E)-geranyllinalool. The first step of both pathways, the formation of the tertiary terpene alcohols (E,E)-geranyllinalool and (E)-nerolidol, is catalyzed by the terpene synthase, TPS2, whereas the subsequent oxidative degradation to DMNT and TMTT is catalyzed by two specific P450 monooxygenases, CYP92C5 and CYP92C6. Pathway mapping of 26 parent lines of US-NAM population for pathways and enzymes contributing to volatile terpene biosynthesis in maize leaves. TPS2 is the regulatory key enzyme
physiological function
enzyme CYP82G1 produces (3E)-4,8-dimethylnona-1,3,7-triene, DMNT, and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT, in vitro but functions as a TMTT synthase in planta because of the presence of (E,E)-geranyllinalool but not of (E)-nerolidol in Arabidopsis thaliana leaves
physiological function
B6ST66, B8A110
gene disruption of CYP92C5 results in loss of (3E)-4,8-dimethylnona-1,3,7-triene production and reduced levels of (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene after simulated herbivory. In planta (3E)-4,8-dimethylnona-1,3,7-triene is primarily produced by isoform CYP92C5, whereas the majority of (3E,7E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene is produced by cytochrome P450 monooxygenase, CYP92C6
physiological function
while Arabidopsis thaliana and other angiosperms are known to produce the homoterpene (E)-4,8-dimethyl-1,3,7-nonatriene, DMNT, or its C16-analogue (E,E)-4,8,12-trimethyl-1,3,7,11-tridecatetraene, TMTT, by the breakdown of sesquiterpene and diterpene tertiary alcohols in aboveground tissues, Arabidopsis thaliana roots biosynthesize DMNT by the degradation of the C30 triterpene diol, arabidiol. The reaction is catalyzed by the Brassicaceae-specific cytochrome P450 monooxygenase CYP705A1. In volatile terpene biosynthesis, irregular homo/norterpenes can arise from different biosynthetic routes in a tissue-specific manner. DMNT negatively affects pathogen Pythium irregulare oospore germination and growth
physiological function
B6ST66, B8A110
while enzyme CYP92C5 converts (E)-nerolidol and (E,E)-geranyllinalool to (3E)-4,8-dimethyl-1,3,7,-nonatriene (DMNT) and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, respectively, enzyme CYP92C6 only converts (E,E)-geranyllinalool to (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT. (E)-4,8-Dimethyl-1,3,7-nonatriene, DMNT, and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT, are volatile homoterpenes. Many such volatiles are assigned functions in the defense against pathogens like lepidopteran larvae, aphids, fungi,and bacteria. Maize volatiles released after herbivore damage display high levels of quantitative and qualitative variation. In planta, DMNT is primarily produced by CYP92C5, whereas the majority of TMTT is produced by a related cytochrome P450 monooxygenase, CYP92C6, which is specific for the conversion of (E,E)-geranyllinalool to TMTT
physiological function
B6ST66, B8A110
while enzyme CYP92C5 converts (E)-nerolidol and (E,E)-geranyllinalool to DMNT and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, respectively, enzyme CYP92C6 only converts (E,E)-geranyllinalool to (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT. (E)-4,8-Dimethyl-1,3,7-nonatriene, DMNT, and (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene, TMTT, are volatile homoterpenes. Many such volatiles are assigned functions in the defense against pathogens like lepidopteran larvae, aphids, fungi,and bacteria. Maize volatiles released after herbivore damage display high levels of quantitative and qualitative variation. In planta, DMNT is primarily produced by CYP92C5, whereas the majority of TMTT is produced by a related cytochrome P450 monooxygenase, CYP92C6, which is specific for the conversion of (E,E)-geranyllinalool to TMTT
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). C82G1_ARATH
515
1
58570
Swiss-Prot
Secretory Pathway (Reliability: 1)
C92C5_MAIZE
531
1
57704
Swiss-Prot
Secretory Pathway (Reliability: 4)
C92C6_MAIZE
554
1
60524
Swiss-Prot
Chloroplast (Reliability: 4)
A0A7L5BC44_ORYSA
478
0
53595
TrEMBL
Mitochondrion (Reliability: 5)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling and substrate docking support an oxidative bond cleavage of the alcohol substrate via syn-elimination of the polar head, together with an allylic C-5 hydrogen atom
molecular docking of (E,E)-geranyllinalool and (E)-nerolidol shows that both substrates occupiy the same position in the enzyme binding site with the hydroxyl group at C-3, forming a strong hydrogen bond to the carbonyl oxygen of Thr313. The position of the allylic hydrogen atoms at C-5 of (E,E)-geranyllinalool and (E)-nerolidol and the hydroxyl group at C-3 relative to the reactive iron-oxo heme moiety supports an oxidative-bond cleavage reaction proceeding by a syn-elimination mechanism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of the cyp705a1-1 null mutant, the mutant is complemented with a full-length CYP705A1 cDNA in C-terminal fusion to enhanced yellow fluorescent protein (eYFP)
additional information
construction of the cyp705a1-1 null mutant, the mutant is complemented with a full-length CYP705A1 cDNA in C-terminal fusion to enhanced yellow fluorescent protein (eYFP)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the yeast expression vector YEp352 under the control of the constitutive alcohol dehydrogenase 1 promoter, expression in yeast
gene CYP705A1, the full-length CYP705A1 transcript is fused to the CaMV 35S promoter for ectopic expression in the cyp705a1-1 mutant background
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP705A1 is transiently induced in a jasmonate-dependent manner by infection with the root rot oomycete pathogen Pythium irregulare. DMNT is emitted from Arabidopsis thaliana roots upon infection with Pythium irregulare or treatment with jasmonic acid. ProCYP705A1:CYP705A1-eYFP lines, accumulation of the full-length CYP705A1 transcript is detected upon JA treatment, while only basal transcript levels of the gene are observed in ProCaMV35S-CYP705A1 lines with no jasmonate-dependent increase of transcript abundance
CYP82G1 is induced in Arabidopsis thaliana leaves upon insect feeding damage
expression of CYP82G1 is induced by treatment with alamethicin, coronalon and at sites of feeding damage by larvae of P. xylostella
-
highly coordinated herbivore-induced expression with geranyllinalool synthase in leaves depending on the F-box protein COI-1. Induction of CYP82G1 in response to feeding by Pseudomonas xylostella larvae and upon infection with Pseudomonas syringae DC3000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, S.; Badieyan, S.; Bevan, D.R.; Herde, M.; Gatz, C.; Tholl, D.
Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis
Proc. Natl. Acad. Sci. USA
107
21205-21210
2010
Arabidopsis thaliana (Q9LSF8)
brenda
Tholl, D.; Sohrabi, R.; Huh, J.; Lee, S.
The biochemistry of homoterpenes - Common constituents of floral and herbivore-induced plant volatile bouquets
Phytochemistry
72
1635-1646
2011
Arabidopsis thaliana
brenda
Sohrabi, R.; Huh, J.; Badieyan, S.; Rakotondraibe, L.; Kliebenstein, D.; Sobrado, P.; Tholl, D.
In planta variation of volatile biosynthesis an alternative biosynthetic route to the formation of the pathogen-induced volatile homoterpene DMNT via triterpene degradation in Arabidopsis roots
Plant Cell
27
874-890
2015
Arabidopsis thaliana, Arabidopsis thaliana (B0T7D7)
brenda
Richter, A.; Schaff, C.; Zhang, Z.; Lipka, A.; Tian, F.; Koellner, T.; Schnee, C.; Preiss, S.; Irmisch, S.; Jander, G.; Boland, W.; Gershenzon, J.; Buckler, E.; Degenhardt, J.
Characterization of biosynthetic pathways for the production of the volatile homoterpenes DMNT and TMTT in Zea mays
Plant Cell
28
2651-2665
2016
Zea mays, Zea mays (B6ST66), Zea mays (B8A110)
brenda
Lee, S.; Badieyan, S.; Bevan, D.R.; Herde, M.; Gatz, C.; Tholl, D.
Herbivore-induced and floral homoterpene volatiles are biosynthesized by a single P450 enzyme (CYP82G1) in Arabidopsis
Proc. Natl. Acad. Sci. USA
107
21205-21210
2010
Arabidopsis thaliana (Q9LSF8)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.14.58)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
