Information on EC 1.1.1.319 - isoeugenol synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.319
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RECOMMENDED NAME
GeneOntology No.
isoeugenol synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isoeugenol + acetate + NADP+ = coniferyl acetate + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
eugenol and isoeugenol biosynthesis
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Phenylpropanoid biosynthesis
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phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
eugenol:NADP+ oxidoreductase (coniferyl acetate reducing)
The enzyme acts in the opposite direction. In Ocimum basilicum (sweet basil), Clarkia breweri and Petunia hybrida only isoeugenol is formed [1,2]. However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
no activity in Larrea tridentata
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the phenylpropene-forming isoeugenol, IGS, synthase belongs to a structural family of NADPH-dependent reductases that also includes eugenol synthase, EGS, pinoresinol–lariciresinol reductase, isoflavone reductase, and phenylcoumaran benzylic ether reductase, evolution and function of EGS1 and IGS1, overview
malfunction
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the IGS gene of Petunia axillaris subsp. parodii contains a frame-shift mutation that renders it inactive. In the absence of IGS activity the coniferyl acetate substrate is converted to dihydroconiferyl acetate, instead that eugenol synthesis is increased, overview
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaryl acetate + NADPH + H+
t-anol + acetate + NADP+
show the reaction diagram
coniferyl acetate + NADPH + H+
isoeugenol + acetate + NADP+
show the reaction diagram
additional information
?
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the position of the substrate in the active site of PhIGS1 is such that the hydride is transferred to C9 instead of C7, as occurs in Ocimum basilicum eugenol synthase, EC 1.1.1.318
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-coumaryl acetate + NADPH + H+
t-anol + acetate + NADP+
show the reaction diagram
coniferyl acetate + NADPH + H+
isoeugenol + acetate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
weak inhibition at 2.5 mM
Cu2+
strong inhibition at 2.5 mM
Fe2+
strong inhibition at 2.5 mM
K+
weak inhibition at 2.5 mM
Mn2+
weak inhibition at 2.5 mM
Zn2+
strong inhibition at 2.5 mM
additional information
no inhibitory effect on the activity with 2.5 mM Na+ or Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.134
4-coumaryl acetate
pH 7.5, 25°C
0.2115 - 0.23
coniferyl acetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
4-coumaryl acetate
Pimpinella anisum
B8RCD2
pH 7.5, 25°C
0.99 - 1.3
coniferyl acetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
4-coumaryl acetate
Pimpinella anisum
B8RCD2
pH 7.5, 25°C
15224
4.44 - 5.7
coniferyl acetate
4187
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.65
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purified native, wild-type CbIGS1, pH 6.5, 28°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
developing
Manually annotated by BRENDA team
additional information
the gene encoding AIS1 is expressed throughout the plant, its transcript level is highest in developing fruits
Manually annotated by BRENDA team
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
purified recombinant enzyme, 30 min, stable
37
purified recombinant enzyme, 30 min, 85% activity remaining
50
purified recombinant enzyme, 30 min, nelow 45 activity remaining
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 9.2fold from petals by alternating steps of anion exchange and hydrophobic interaction chromatography, co-purification with eugenol synthase, EC 1.1.1.318. Recombinant His-tagged CbIGS from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Escherichia coli
DNA and amino acid sequence determination and analysis, sequence comparison, quantitative expression analysis
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DNA and amino acid sequence determination and analysis, sequence comparison, quantitative expression analysis, levels of PapIGS transcripts are extremely low
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression in Escherichia coli
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative expression analysis
IGS1 expression in Fragaria x ananassa cv. Elsanta via transfection with Agrobacterium tumefaciens strain AGL0, downregulation of chalcone synthase via antisense construct in parallel
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L91I/L92H/D95N
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
R73K/V77I/S83P/V84F
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
R73K/V77I/S83P/V84F/Y87I/P88S/L91I/L92H/D95N
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
S83P/V84F
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
S83P/V84F/Y87I/P88S
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
V84F
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
V84F/Y87I
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
Y87I
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
Y87I/P88S
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
V88F/Y91I
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site-directed mutagenesis, the mutant plants show increased eugenol production and an altered eugenol/isoeugenol ratio compared to the wild-type enzyme
additional information
recombinant Petunia hybrida IGS expression alone does not increase the concentration of anol or isoeugenol in agroinfiltrated strawberry fruits, concurrent silencing of CHS substantially enhances the yield of the two metabolites