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Information on EC 2.1.1.136 - chlorophenol O-methyltransferase
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2.1.1.136 chlorophenol O-methyltransferaseIUBMB Comments
The enzyme from the fungus Trichoderma sp. virgatum, when cultured in the presence of halogenated phenol, also acts on a range of mono-, di- and trichlorophenols.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
chlorophenol o-methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPOMT
halogenated phenol O-methyltransferase
-
-
-
-
trichlorophenol O-methyltransferase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:trichlorophenol O-methyltransferase
The enzyme from the fungus Trichoderma sp. virgatum, when cultured in the presence of halogenated phenol, also acts on a range of mono-, di- and trichlorophenols.
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CAS REGISTRY NUMBER
COMMENTARY
196414-37-6
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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
2,3,4,5-tetrachlorophenol + S-adenosyl-L-methionine
2,3,4,5-tetrachloroanisole + S-adenosyl-L-homocysteine
2,3,4-trichlorophenol + S-adenosyl-L-methionine
2,3,4-trichloroanisole + S-adenosyl-L-homocysteine
2,3,6-trichlorophenol + S-adenosyl-L-methionine
2,3,6-trichloroanisole + S-adenosyl-L-homocysteine
2,3-dichlorophenol + S-adenosyl-L-methionine
2,3-dichloroanisole + S-adenosyl-L-homocysteine
-
22.5% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4,5-trichlorophenol + S-adenosyl-L-methionine
2,4,5-trichloroanisole + S-adenosyl-L-homocysteine
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64.2% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4,6-tribromophenol + S-adenosyl-L-methionine
2,4,6-tribromoanisole + S-adenosyl-L-homocysteine
-
13% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
2,4-dibromophenol + S-adenosyl-L-methionine
2,4-dibromoanisole + S-adenosyl-L-homocysteine
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36.8% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4-dichlorophenol + S-adenosyl-L-methionine
2,3-dichloroanisole + S-adenosyl-L-homocysteine
-
-
-
-
?
2,5-dichlorophenol + S-adenosyl-L-methionine
2,5-dichloroanisole + S-adenosyl-L-homocysteine
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19.6% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,6-dichlorophenol + S-adenosyl-L-methionine
2,6-dichloroanisole + S-adenosyl-L-homocysteine
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10.4% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2-chlorophenol + S-adenosyl-L-methionine
2-chloroanisole + S-adenosyl-L-homocysteine
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9.6% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
3,4-dichlorophenol + S-adenosyl-L-methionine
3,4-dichloroanisole + S-adenosyl-L-homocysteine
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9.3% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
S-adenosyl-L-methionine + 2,4,6-trichlorophenol
S-adenosyl-L-homocysteine + 2,4,6-trichloroanisole
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-
-
-
?
trichlorophenol + S-adenosyl-L-methionine
trichloroanisole + S-adenosyl-L-homocysteine
-
-
-
?
2,3,4,5-tetrachlorophenol + S-adenosyl-L-methionine
2,3,4,5-tetrachloroanisole + S-adenosyl-L-homocysteine
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10.7% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,3,4,5-tetrachlorophenol + S-adenosyl-L-methionine
2,3,4,5-tetrachloroanisole + S-adenosyl-L-homocysteine
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10.7% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,3,4-trichlorophenol + S-adenosyl-L-methionine
2,3,4-trichloroanisole + S-adenosyl-L-homocysteine
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93.3% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,3,4-trichlorophenol + S-adenosyl-L-methionine
2,3,4-trichloroanisole + S-adenosyl-L-homocysteine
-
93.3% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,3,6-trichlorophenol + S-adenosyl-L-methionine
2,3,6-trichloroanisole + S-adenosyl-L-homocysteine
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55.6% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,3,6-trichlorophenol + S-adenosyl-L-methionine
2,3,6-trichloroanisole + S-adenosyl-L-homocysteine
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55.6% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
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activity is induced by 2,4,6-trichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
-
60% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
-
activity is induced by 2,4,6-trichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
-
60% of the O-methylation activity with 2,3-dichlorophenol
-
-
?
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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
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
trichlorophenol + S-adenosyl-L-methionine
trichloroanisole + S-adenosyl-L-homocysteine
-
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
-
activity is induced by 2,4,6-trichlorophenol
-
-
?
2,4,6-trichlorophenol + S-adenosyl-L-methionine
2,4,6-trichloroanisole + S-adenosyl-L-homocysteine
-
activity is induced by 2,4,6-trichlorophenol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-methyltetrahydrofolic acid
-
1 mM, activation to 119% of control
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
pH 7.0: about 50% of maximal activity, pH 7.0-8.5: optimum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme acts also on a range of mono-, di- and trichlorophenols
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is responsible for the detoxification of chlorophenolic pesticides by O-methylation which results in the formation of chloroanisoles
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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). CMT1_TRILO
467
0
52461
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
partial silencing of cmt1 gene results in a 48.9% decrease of enzyme activity levels in a Trichoderma longibrachiatum At37 transformant strain by comparison with the wild type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
54% loss of activity after 30 min, 89% loss of activity after 1 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing of the purified or semipurified enzymic preparation results in almost complete loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography. hydroxyapatite column chromatography, Resource Q column chromatography, ultrafiltration, and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of the enzyme is induced at transcriptional level by exposure of fungal mycelia to 0.01 mg/ml 2,4,6-trichlorophenol
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kikuchi, T.; Oe, T.
Halogenated phenol O-methyltransferase, its preparation from Trichoderma and methods for wood products deodorization
Jpn. Kokai Tokkyo Koho
8
1996
Trichoderma virgatum (nom. inval.)
-
brenda
Coque, J.J.; Alvarez-Rodriguez, M.L.; Larriba, G.
Characterization of an inducible chlorophenol O-methyltransferase from Trichoderma longibrachiatum involved in the formation of chloroanisoles and determination of its role in cork taint of wines
Appl. Environ. Microbiol.
69
5089-5095
2003
Trichoderma longibrachiatum, Trichoderma longibrachiatum CECT 20431
brenda
Feltrer, R.; Alvarez-Rodriguez, M.L.; Barreiro, C.; Godio, R.P.; Coque, J.J.
Characterization of a novel 2,4,6-trichlorophenol-inducible gene encoding chlorophenol O-methyltransferase from Trichoderma longibrachiatum responsible for the formation of chloroanisoles and detoxification of chlorophenols
Fungal Genet. Biol.
47
458-467
2010
Trichoderma longibrachiatum
brenda
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