BRENDA - Enzyme Database show
show all sequences of 2.1.1.165

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
Raphanus sativus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.19
-
S-adenosyl-L-methionine
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
4.47
-
Iodide
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
177.3
-
bromide
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
1657
-
chloride
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27500
-
x * 27500, calculated from sequence
Raphanus sativus
29000
-
x * 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
partial
Raphanus sativus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Raphanus sativus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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 thiol methyltransferase activity (EC 2.1.1.9), high activity towards SCN-
696997
Raphanus sativus
?
-
-
-
-
S-adenosyl-L-methionine + bromide
production rate of bromomethane is 24fold lower than production rate of iodomethane
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
?
S-adenosyl-L-methionine + chloride
production rate of chloromethane is 925fold lower than production rate of iodomethane
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
?
S-adenosyl-L-methionine + iodide
iodide is the preferred substrate
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
?
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
Raphanus sativus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.19
-
S-adenosyl-L-methionine
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
4.47
-
Iodide
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
177.3
-
bromide
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
1657
-
chloride
pH 7.0, 30°C, purified recombinant enzyme
Raphanus sativus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27500
-
x * 27500, calculated from sequence
Raphanus sativus
29000
-
x * 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
partial
Raphanus sativus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Raphanus sativus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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 thiol methyltransferase activity (EC 2.1.1.9), high activity towards SCN-
696997
Raphanus sativus
?
-
-
-
-
S-adenosyl-L-methionine + bromide
production rate of bromomethane is 24fold lower than production rate of iodomethane
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
?
S-adenosyl-L-methionine + chloride
production rate of chloromethane is 925fold lower than production rate of iodomethane
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
?
S-adenosyl-L-methionine + iodide
iodide is the preferred substrate
696997
Raphanus sativus
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 27500, calculated from sequence; x * 29000, SDS-PAGE
Raphanus sativus
Other publictions for EC 2.1.1.165
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)
696997
Itoh
Involvement of S-adenosylmethi ...
Raphanus sativus
BMC Plant Biol.
9
116
2009
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-
1
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4
-
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2
1
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1
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1
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1
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5
1
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1
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4
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1
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1
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1
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5
1
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-
-
-
-
698496
Bayer
Synthesis of methyl halides fr ...
Batis maritima, Brassica rapa, Burkholderia pseudomallei, Burkholderia thailandensis, Oryza sativa, Paraburkholderia phytofirmans, Paraburkholderia xenovorans, Vitis vinifera
J. Am. Chem. Soc.
131
6508-6515
2009
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8
8
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16
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21
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8
8
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21
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698916
Nagatoshi Y
Arabidopsis HARMLESS TO OZONE ...
Arabidopsis thaliana
J. Biol. Chem.
284
19301-19309
2009
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-
-
-
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-
-
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1
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3
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1
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700702
Nagatoshi. Y.; Nakamura
-
Characterization of three hali ...
Arabidopsis thaliana
Plant Biotechnol.
24
503-506
2007
-
-
1
-
-
-
-
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2
3
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3
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3
3
9
1
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3
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3
3
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3
3
9
3
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-
679357
Rhew
Genetic control of methyl hali ...
Arabidopsis thaliana
Curr. Biol.
13
1809-1813
2003
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-
1
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1
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1
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1
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1
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1
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695730
Amachi
Bacteria mediate methylation o ...
Rhizobium sp., Rhizobium sp. MRCD 19
Appl. Environ. Microbiol.
67
2718-2722
2001
-
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1
2
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2
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2
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2
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1
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4
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1
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-
1
-
-
-
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-
-
-
-
-
696802
Ohsawa
Purification and characterizat ...
Pavlova pinguis
Biosci. Biotechnol. Biochem.
65
2397-2404
2001
-
-
-
-
-
-
14
2
-
1
1
-
-
2
-
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1
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1
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4
1
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1
1
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1
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14
-
2
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1
1
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1
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1
-
4
1
-
-
-
-
1
1
-
1
-
-
-
-
-
-
682595
Ni
Expression of Batis maritima m ...
Batis maritima
Proc. Natl. Acad. Sci. USA
96
3611-3615
1999
1
-
1
-
-
-
1
8
-
1
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1
-
5
-
-
-
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4
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3
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1
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1
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1
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8
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1
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1
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4
-
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-
-
3
-
-
-
-
-
-
-
-
-
677650
Saxena
Biochemical characterization o ...
Phellinus pomaceus
Appl. Environ. Microbiol.
64
2831-2835
1998
-
-
-
-
-
-
1
4
1
-
-
1
-
3
-
-
1
-
-
1
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1
4
-
-
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-
1
1
-
1
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-
1
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1
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4
1
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1
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1
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1
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1
4
-
-
-
-
-
1
1
-
-
-
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-
-
-
-
682593
Ni
cDNA cloning of Batis maritima ...
Batis maritima
Proc. Natl. Acad. Sci. USA
95
12866-12871
1998
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-
1
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1
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3
1
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3
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1
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1
1
1
4
1
1
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1
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1
1
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1
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3
1
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1
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1
1
1
4
1
1
-
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1
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-
1
-
-
-
-
-
-
700660
Itoh
-
Formation and emission of mono ...
Papenfussiella kuromo, Pavlova gyrans, Sargassum horneri
Phytochemistry
45
67-73
1997
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-
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1
2
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3
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3
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4
8
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1
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1
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1
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4
8
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1
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1
1
-
-
-
-
-
-
-
-
680600
Attieh
Purification and characterizat ...
Brassica oleracea
J. Biol. Chem.
270
9250-9257
1995
-
-
-
-
-
-
2
4
-
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2
-
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2
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1
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1
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4
4
1
1
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1
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2
1
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2
2
4
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2
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1
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1
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4
4
1
1
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1
-
-
1
-
-
-
-
-
-
700704
Saini
-
Biosynthesis of halomethanes a ...
Brassica oleracea
Plant Cell Environ.
18
1027-1033
1995
-
-
-
-
-
-
-
-
-
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1
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4
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4
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701215
Wuosmaa
Methyl chloride transferase: a ...
Endocladia muricata
Science
249
160-162
1990
-
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2
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1
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4
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