HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 4.2.3.61 - 5-epiaristolochene synthase
for references in articles please use BRENDA:EC4.2.3.61Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
4.2.3.61
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
5-epiaristolochene 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
(2E,6E)-farnesyl diphosphate = (+)-5-epiaristolochene + diphosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate diphosphate-lyase [(+)-5-epiaristolochene-forming]
Initial cyclization gives (+)-germacrene A in an enzyme bound form which is not released to the medium.
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.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
(2E,6E)-farnesyl diphosphate
5-epi-aristolochene + diphosphate
-
-
-
?
(2E,6Z)-6-fluorofarnesyl diphosphate
(-)-1-fluorogermacrene A
-
the fluoro substitution at the C6 position of farnesyl diphosphate has negligible effects on enzyme binding, substrate orientation, diphosphate ionization, and the initial 1,10 ring closure catalyzed by TEAS
sole product, 58% yield
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
-
single major sesquiterpene product
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
-
-
(+)-5-epiaristolochene constitutes about 85% of hyxdrocarbon products
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
-
-
about 79% of hydrocarbon product, plus about 6% of (-)-4-epi-eremophilene, 3.6% of (+)-germacrene A and 22 hydrocarbons contributing about 12% of TEAS sesquiterpene products. The pathway to the by-products starts with a 1,6 cyclization of the (Z,E)-farnesyl cation, followed by a 1,2 hydride shift leading to a syn-6,10 ring closure which generates an acoradilyl cation. Elimination of a proton from either C12 or C13 of the isopropylidene tail of the acoradilyl cation readily explains the formation of ?-acoradiene. Alternatively, a 2,11 ring closure followed by elimination of a proton at C2 is the likely pathway to (-)-alpha-cedrene. A 3,11 ring closure of the acoradilyl cation is the most common event, based on the relative abundance of isomerization products observed, and is followed by Wagner-Meerwein rearrangement and proton elimination from C15 to produce isoprezizaene, the dominant (Z,E)-farnesyl cation-derived product
-
?
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
reaction proceeds via geracrene A as an intermediate. Proton donation by residue Y520 is responsible for the activation of germacrene A to a eudesmane cation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.0016
(2E,6E)-farnesyl diphosphate
-
fusion construct epiaristolochene synthase/farnesyl diphosphate synthase, pH 8.0, 30°C
0.0026
(2E,6E)-farnesyl diphosphate
-
fusion construct farnesyl diphosphate synthase/epiaristolochene synthase, pH 8.0, 30°C
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
no constitutive expression of EAS and capsidiol accumulation in shoots of rosette plants, but accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta
additional information
no constitutive expression of EAS and capsidiol accumulation in shoots of rosette plants, but accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta
additional information
no constitutive expression of EAS and capsidiol accumulation in shoots of rosette plants, but accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Common tobacco;
Nicotiana tabacum;
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.2-2.8 A resolution, of TEAS alone and in complexes with two different substrate analogs. TEAS consists entirely of alpha-helices and short connecting loops and turns, and is organized into two structural domains. Two Mg2+ ions are coordinated on opposite sides of the entrance to the active site pocket, and constitute a diphosphate binding site. Asp301 coordinates a Mg2+ in the native TEAS structure, and the side chain carboxyl of Glu379 provides a longer range interaction. Asp305 provides an additional coordination bond in the enzyme with substrate analogs bound. Asp301 and Asp305 are part of a -DDXXD- sequence. Asp301 directly contacts Mg2+, whereas Asp302 demonstrates no direct metal coordination. The side chains of Asp444, Thr448, Glu452, and one water molecule the second coordinate Mg2+. In the native TEAS structure, the A-C and J-K loops and the residues NH2-terminal of residue 36 are disordered
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Petunia hybrida infiltrated with Agrobacterium tumefaciens harboring the enzyme gene
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta; accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta; accumulation of transcripts can be induced in shoots by feeding of the tobacco hornworm, Manduca sexta
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y520F
-
3% of wild-type catalytic efficiency, reaction prooduct is germacrene A
additional information
additional information
-
heterologous expression of EAS in transgenic rice does not interfere with the activities of endogenous squalene synthase or farnesyl diphosphatase. The induction of EAS enzyme activity is accompanied by an increase in EAS mRNA when challenged by the elicitor. The EAS ectopic expression in transgenic rice plants results in the synthesis of 5-epi-aristolochene in vivo upon elicitor treatment
additional information
-
construction of fusion proteins with farnesyl diphosphate synthase FPPS from Artemisia annua. The fusion enzymes produce epi-aristolochene from isopentenyl diphosphate through a coupled reaction. The Km values of FPPS and eAS for isopentenyl diphosphate and farnesyl diphosphate, respectively, are essentially the same for the single and fused enzymes. The bifunctional enzymes show a more efficient conversion of isopentenyl diphosphate to epi-aristolochene than the corresponding amount of single enzymes
additional information
-
engineering of a thermostable mutant by SCADS algorithm to suggest mutations based on side-chain interactions consistent with the nearby protein backbone, neighboring sidechains, and the local environment, and by replacement of solvent-exposed hydrophobic residues and the addition of salt bridges on the surface of the mutant enzyme. Contrary to wild-type, mutant is still active to 65°C but produces additional sesquiterpene products
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
method for the recovery of full-length cDNAs from predicted terpene synthase genes containing introns. The approach utilizes Agrobacterium-mediated transient expression coupled with a reverse transcription-polydeoxyribonucleotide chain reaction assay to facilitate expression cloning of processed transcripts. Subsequent expression of intronless cDNAs in a suitable prokaryotic host provides for direct functional testing of the encoded gene product
synthesis
synthesis
-
expression system in Escherichia coli, highest expression level after 3 h induction with low concentration of IPTG and incubation at 27°C. Epiaristolochene synthase protein constitutes up to 35% of total Escherichia coli proteins
synthesis
-
construction of fusion proteins with farnesyl diphosphate synthase FPPS from Artemisia annua. The fusion enzymes produce epi-aristolochene from isopentenyl diphosphate through a coupled reaction. The Km values of FPPS and eAS for isopentenyl diphosphate and farnesyl diphosphate, respectively, are essentially the same for the single and fused enzymes. The bifunctional enzymes show a more efficient conversion of isopentenyl diphosphate to epi-aristolochene than the corresponding amount of single enzymes
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.
LINKS TO OTHER DATABASES (specific for EC-Number 4.2.3.61)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
