Information on EC 2.1.1.279 - trans-anol O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.279
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RECOMMENDED NAME
GeneOntology No.
trans-anol O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + isomethyleugenol
show the reaction diagram
S-adenosyl-L-methionine + trans-anol = S-adenosyl-L-homocysteine + trans-anethole
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
epoxypseudoisoeugenol-2-methylbutanoate biosynthesis
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Phenylpropanoid biosynthesis
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t-anethole biosynthesis
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volatile cinnamoic ester biosynthesis
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phenylpropanoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:trans-anol O-methyltransferase
The enzyme from anise (Pimpinella anisum) is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8, and, in contrast to EC 2.1.1.146, (iso)eugenol O-methyltransferase, does not have activity with eugenol or chavicol.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
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
S-adenosyl-L-methionine +
S-adenosyl-L-homocysteine + ?
show the reaction diagram
shows a 10fold preference for isoeugenol over eugenol The enzyme is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8
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?
S-adenosyl-L-methionine + chavicol
S-adenosyl-L-homocysteine + ?
show the reaction diagram
the enzyme shows a 10fold preference for t-anol over chavicol. The enzyme is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8
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-
?
S-adenosyl-L-methionine + isoeugenol
S-adenosyl-L-homocysteine + isomethyleugenol
show the reaction diagram
the enzyme prefers isoeugenol to t-anol by a factor of 2. The enzyme is highly specific for substrates in which the double bond in the propenyl side chain is located between C7 and C8
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-
?
S-adenosyl-L-methionine + trans-anol
S-adenosyl-L-homocysteine + trans-anethole
show the reaction diagram
additional information
?
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the enzyme does not have activity with eugenol or chavicol
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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
S-adenosyl-L-methionine + trans-anol
S-adenosyl-L-homocysteine + trans-anethole
show the reaction diagram
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
2.5 mM, 97% inhibition
Fe2+
2.5 mM, 47% inhibition
Mn2+
2.5 mM, 35% inhibition
Zn2+
2.5 mM, 97% inhibition
additional information
no inhibitory effect on the activity is observed by incubation with 2.5 mM K+, Na+, Ca2+, and Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0193
Isoeugenol
pH 7.5, 25C
0.004 - 0.0545
S-adenosyl-L-methionine
0.032
trans-anol
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in 50 mM bis-Tris pH 7.0, at 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
Isoeugenol
Pimpinella anisum
B8RCD3
pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
Isoeugenol
Pimpinella anisum
B8RCD3
pH 7.5, temperature not specified in the publication
3640
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
Tris buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
active in the range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
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he reaction rate increases with temperature up to 25C, remains roughly constant till reaching 37C and at 45C activity dramatically decreases
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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lowest expression
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
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x * 80000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 80000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
30 min, stable
50
30 min, 12% loss of activity
65
30 min, less than 5% of activity remaining
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Sephadex G-25 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in developing fruits, enzyme activity levels increase until the wasty stage is reached and then dramatically decrease. Young leaves display higher levels of enzyme activity than old leaves
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