BRENDA - Enzyme Database
show all sequences of 2.1.1.9

Involvement of S-adenosylmethionine-dependent halide/thiol methyltransferase (HTMT) in methyl halide emissions from agricultural plants: isolation and characterization of an HTMT-coding gene from Raphanus sativus (daikon radish)

Itoh, N.; Toda, H.; Matsuda, M.; Negishi, T.; Taniguchi, T.; Ohsawa, N.; BMC Plant Biol. 9, 116 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; expressed in Escherichia coli BL21(DE3) cells
Raphanus sativus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
thiocyanate
in 20 mM MES (pH 7.0), at 30°C; pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
0.19
-
S-adenosyl-L-methionine
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
4.47
-
Iodide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
12.24
-
bisulfide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
12.24
-
SH-
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
177.3
-
bromide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
1657
-
chloride
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27500
-
calculated from amino acid sequence
Raphanus sativus
29000
-
SDS-PAGE
Raphanus sativus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Raphanus sativus
the enzyme may be involved in the detoxification of sulfur compounds produced by the degradation of glucosinolates to release them as volatile compounds. The volatile sulfur compounds, including CH3SH and CH3SCN and methyl halides, are believed to act as insecticidal or anti-pathogenic agents. Therefore, it is speculated that the enzyme plays a role in controlling the levels of anions that can inhibit metabolic enzymes in the leaves and also to protect them from damage caused by insects or pathogens
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Raphanus sativus
C6L2E7
-
-
Purification (Commentary)
Commentary
Organism
DEAE-Toyopearl 650 M column chromatography and Ni-Sepharose column chromatography; partial
Raphanus sativus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
; highest activity in mature leaves
Raphanus sativus
-
additional information
no activity in mature roots
Raphanus sativus
-
stem
-
Raphanus sativus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bisulfide + S-adenosyl-L-methionine
highest activity
696997
Raphanus sativus
methanethiol + S-adenosyl-L-homocysteine
-
-
-
?
additional information
the enzyme may be involved in the detoxification of sulfur compounds produced by the degradation of glucosinolates to release them as volatile compounds. The volatile sulfur compounds, including CH3SH and CH3SCN and methyl halides, are believed to act as insecticidal or anti-pathogenic agents. Therefore, it is speculated that the enzyme plays a role in controlling the levels of anions that can inhibit metabolic enzymes in the leaves and also to protect them from damage caused by insects or pathogens
696997
Raphanus sativus
?
-
-
-
-
additional information
the enzyme also shows halide methyltransferase activity
696997
Raphanus sativus
?
-
-
-
-
additional information
the enzyme shows no activity towards CN-
696997
Raphanus sativus
?
-
-
-
-
S-adenosyl-L-methionine + bromide
-
696997
Raphanus sativus
S-adenosyl-L-homocysteine + bromomethane
-
-
-
?
S-adenosyl-L-methionine + chloride
very low activity
696997
Raphanus sativus
S-adenosyl-L-homocysteine + chloromethane
-
-
-
?
S-adenosyl-L-methionine + HS-
-
696997
Raphanus sativus
?
-
-
-
?
S-adenosyl-L-methionine + iodide
-
696997
Raphanus sativus
S-adenosyl-L-homocysteine + iodomethane
-
-
-
?
thiocyanate + S-adenosyl-L-methionine
-
696997
Raphanus sativus
?
-
-
-
?
thiocyanate + S-adenosyl-L-methionine
-
696997
Raphanus sativus
methyl thiocyanate + S-adenosyl-L-homocysteine
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 27500, calculated from sequence; x * 29000, SDS-PAGE
Raphanus sativus
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; expressed in Escherichia coli BL21(DE3) cells
Raphanus sativus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
thiocyanate
in 20 mM MES (pH 7.0), at 30°C; pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
0.19
-
S-adenosyl-L-methionine
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
4.47
-
Iodide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
12.24
-
bisulfide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
12.24
-
SH-
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
177.3
-
bromide
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
1657
-
chloride
in 20 mM MES (pH 7.0), at 30°C
Raphanus sativus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27500
-
calculated from amino acid sequence
Raphanus sativus
29000
-
SDS-PAGE
Raphanus sativus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Raphanus sativus
the enzyme may be involved in the detoxification of sulfur compounds produced by the degradation of glucosinolates to release them as volatile compounds. The volatile sulfur compounds, including CH3SH and CH3SCN and methyl halides, are believed to act as insecticidal or anti-pathogenic agents. Therefore, it is speculated that the enzyme plays a role in controlling the levels of anions that can inhibit metabolic enzymes in the leaves and also to protect them from damage caused by insects or pathogens
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE-Toyopearl 650 M column chromatography and Ni-Sepharose column chromatography; partial
Raphanus sativus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
; highest activity in mature leaves
Raphanus sativus
-
additional information
no activity in mature roots
Raphanus sativus
-
stem
-
Raphanus sativus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bisulfide + S-adenosyl-L-methionine
highest activity
696997
Raphanus sativus
methanethiol + S-adenosyl-L-homocysteine
-
-
-
?
additional information
the enzyme may be involved in the detoxification of sulfur compounds produced by the degradation of glucosinolates to release them as volatile compounds. The volatile sulfur compounds, including CH3SH and CH3SCN and methyl halides, are believed to act as insecticidal or anti-pathogenic agents. Therefore, it is speculated that the enzyme plays a role in controlling the levels of anions that can inhibit metabolic enzymes in the leaves and also to protect them from damage caused by insects or pathogens
696997
Raphanus sativus
?
-
-
-
-
additional information
the enzyme also shows halide methyltransferase activity
696997
Raphanus sativus
?
-
-
-
-
additional information
the enzyme shows no activity towards CN-
696997
Raphanus sativus
?
-
-
-
-
S-adenosyl-L-methionine + bromide
-
696997
Raphanus sativus
S-adenosyl-L-homocysteine + bromomethane
-
-
-
?
S-adenosyl-L-methionine + chloride
very low activity
696997
Raphanus sativus
S-adenosyl-L-homocysteine + chloromethane
-
-
-
?
S-adenosyl-L-methionine + HS-
-
696997
Raphanus sativus
?
-
-
-
?
S-adenosyl-L-methionine + iodide
-
696997
Raphanus sativus
S-adenosyl-L-homocysteine + iodomethane
-
-
-
?
thiocyanate + S-adenosyl-L-methionine
-
696997
Raphanus sativus
?
-
-
-
?
thiocyanate + S-adenosyl-L-methionine
-
696997
Raphanus sativus
methyl thiocyanate + S-adenosyl-L-homocysteine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 27500, calculated from sequence; x * 29000, SDS-PAGE
Raphanus sativus
Other publictions for EC 2.1.1.9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
733711
Liu
Human liver cytochrome P450 en ...
Homo sapiens
Drug Metab. Dispos.
43
1632-1641
2015
-
1
-
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1
-
1
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2
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2
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720650
Takekawa
-
Rice OsHOL1 and OsHOL2 protein ...
Oryza sativa
Plant Biotechnol.
29
103-108
2012
-
-
1
-
-
-
-
2
-
-
2
-
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1
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1
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2
2
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1
1
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2
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2
2
721115
Obach
Reduction and methylation of z ...
Homo sapiens
Xenobiotica
42
1049-1057
2012
-
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1
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1
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723371
Zhao
A SABATH Methyltransferase fro ...
Physcomitrella patens
Phytochemistry
81
31-41
2012
-
-
1
-
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7
2
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1
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5
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1
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4
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1
1
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7
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2
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1
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1
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4
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4
1
1
-
3
-
2
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2
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720635
Toda
Isolation and characterization ...
Phaeodactylum tricornutum, Phaeodactylum tricornutum CCAP 1055/1
Phytochemistry
72
337-343
2011
-
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1
-
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2
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2
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7
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1
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2
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1
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1
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4
1
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2
1
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-
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-
2
2
718580
Schmidberger
Halomethane biosynthesis: Stru ...
Arabidopsis thaliana
Angew. Chem. Int. Ed. Engl.
49
3646-3648
2010
-
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1
1
2
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3
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2
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1
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3
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1
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1
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1
2
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3
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1
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3
-
1
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-
-
-
-
-
-
-
-
-
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696997
Itoh
Involvement of S-adenosylmethi ...
Raphanus sativus
BMC Plant Biol.
9
116
2009
-
-
1
-
-
-
-
7
-
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2
1
-
12
-
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1
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3
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10
1
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1
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7
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1
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1
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3
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10
1
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698916
Nagatoshi Y
Arabidopsis HARMLESS TO OZONE ...
Arabidopsis thaliana
J. Biol. Chem.
284
19301-19309
2009
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676510
Coiner
Methylation of sulfhydryl grou ...
Catharanthus roseus
Plant J.
46
193-205
2006
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1
1
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2
3
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3
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1
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13
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1
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1
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13
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1
1
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1
1
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660223
Kocsis
Insertional inactivation of th ...
Arabidopsis thaliana, Zea mays
Plant Physiol.
131
1808-1815
2003
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2
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2
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2
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441597
Attieh
Cloning and functional express ...
Brassica oleracea
Plant Mol. Biol.
50
511-521
2002
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1
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6
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441356
Kim
Arylamine N-methyltransferase ...
Rattus norvegicus
Exp. Mol. Med.
33
23-28
2001
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1
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696802
Ohsawa
Purification and characterizat ...
Pavlova pinguis
Biosci. Biotechnol. Biochem.
65
2397-2404
2001
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441594
Attieh
Purification and properties of ...
Brassica oleracea
Arch. Biochem. Biophys.
380
257-266
2000
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3
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6
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4
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1
2
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441596
Roediger
Thiol methyltransferase activi ...
Homo sapiens
Gut
47
206-210
2000
-
1
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-
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-
-
-
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2
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1
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700704
Saini
-
Biosynthesis of halomethanes a ...
Brassica oleracea
Plant Cell Environ.
18
1027-1033
1995
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441589
Glauser
Human hepatic microsomal thiol ...
Homo sapiens
Drug Metab. Dispos.
20
247-255
1992
-
-
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
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-
-
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-
-
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-
2
-
-
1
-
-
-
-
-
2
-
-
-
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-
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-
441590
Otterness
Mouse liver thiol methyltransf ...
Mus musculus
Drug Metab. Dispos.
14
680-688
1986
-
-
-
-
-
-
1
1
1
-
-
-
-
5
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
441591
Drotar
-
Methylation of xenobiotic thio ...
Euglena gracilis
Plant Cell Physiol.
26
847-854
1985
-
-
-
-
-
-
-
3
1
-
1
1
-
1
-
-
1
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
3
1
-
1
1
-
-
-
1
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
441587
Weisiger
Thiol S-methyltransferase ...
Rattus norvegicus
Methods Enzymol.
77
257-262
1981
-
-
-
-
-
-
2
16
2
-
1
1
-
1
-
-
1
-
-
4
-
-
15
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
16
2
-
1
1
-
-
-
1
-
4
-
-
15
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
441588
Holloway
Gas chromatographic method for ...
Oryctolagus cuniculus
J. Chromatogr.
202
423-429
1980
-
-
-
-
-
-
-
-
-
-
-
-
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1
-
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1
1
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1
1
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-
-
-
-
441592
Weisiger
Thiol S-methyltransferase: Sug ...
Rattus norvegicus
Biochem. Pharmacol.
29
2885-2887
1980
-
-
-
-
-
-
-
3
-
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1
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1
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1
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3
-
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1
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1
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-
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-
-
-
-
441585
Weisiger
Thiol S-methyltransferase from ...
Rattus norvegicus
Arch. Biochem. Biophys.
196
631-637
1979
-
-
-
-
-
1
1
16
-
-
2
-
-
2
-
-
1
1
-
2
1
-
19
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
16
-
-
2
-
-
-
-
1
-
2
1
-
19
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
441593
Weinshilboum
Human erythrocyte thiol methyl ...
Homo sapiens
Clin. Chim. Acta
97
59-71
1979
-
-
-
-
-
-
1
1
2
1
-
-
-
2
-
-
-
-
-
2
-
-
2
-
-
-
-
-
1
-
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-
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1
-
1
2
1
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
441584
Borchardt
Purification and characterizat ...
Rattus norvegicus
Biochim. Biophys. Acta
522
340-353
1978
-
-
-
-
-
-
6
8
1
1
-
-
-
2
-
-
1
-
-
2
-
1
11
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
6
-
8
1
1
-
-
-
-
-
1
-
2
-
1
11
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
441586
Bremer
-
Enzymic methylation of foreign ...
Bos taurus, Cavia porcellus, Gallus gallus, Mus musculus, Oryctolagus cuniculus, Ovis aries, Rattus norvegicus
Biochim. Biophys. Acta
46
217-224
1961
-
-
-
-
-
-
-
-
7
-
-
-
-
7
-
-
-
-
-
7
-
-
17
-
7
-
-
-
1
-
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-
-
-
-
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-
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7
-
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7
-
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17
-
7
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1
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-