Information on EC 4.2.3.61 - 5-epiaristolochene synthase

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The expected taxonomic range for this enzyme is: Solanaceae

EC NUMBER
COMMENTARY hide
4.2.3.61
-
RECOMMENDED NAME
GeneOntology No.
5-epiaristolochene synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate = (+)-5-epiaristolochene + diphosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
capsidiol biosynthesis
-
-
Sesquiterpenoid and triterpenoid biosynthesis
-
-
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate
(+)-5-epiaristolochene + diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate
5-epi-aristolochene + diphosphate
show the reaction diagram
-
-
-
?
(2E,6Z)-6-fluorofarnesyl diphosphate
(-)-1-fluorogermacrene A
show the reaction diagram
-
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
presence of 2 Mg2+ ions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.014
(2E,6E)-farnesyl diphosphate
0.0197
(2E,6Z)-6-fluorofarnesyl diphosphate
-
pH 7.0, 22C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 0.095
(2E,6E)-farnesyl diphosphate
0.11
(2E,6Z)-6-fluorofarnesyl diphosphate
Nicotiana tabacum
-
pH 7.0, 22C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5 - 6.7
(2E,6E)-farnesyl diphosphate
5.6
(2E,6Z)-6-fluorofarnesyl diphosphate
Nicotiana tabacum
-
pH 7.0, 22C
25175
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
wild-type, no activity above
65
-
thermostable mutant, active up to
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
constitutive expression
Manually annotated by BRENDA team
additional information
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
wild-type, denaturation
83
-
thermostable mutant, denaturation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Oryza sativa
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expression in Petunia hybrida infiltrated with Agrobacterium tumefaciens harboring the enzyme gene
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y520F
-
3% of wild-type catalytic efficiency, reaction prooduct is germacrene A
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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