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S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
additional information
?
-
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
kcat/KM for bromide is 12529fold lower than kcat/Km for iodide
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
very low activity
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
very low activity
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
very low activity
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
the rate of production of methyl bromide is 135fold lower than production of methyl iodide
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
Vmax/Km for bromide is 17fold lower than Vmax/Km for iodide
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
production rate of bromomethane is 24fold lower than production rate of iodomethane
-
-
?
S-adenosyl-L-methionine + bromide
S-adenosyl-L-homocysteine + methyl bromide
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
an obvious function for a halophytic methylase would be the maintenance of homeostatic levels of cytoplasmic chloride ion. The secretion of excess chloride into the soil could not greatly benefit a halophytic plant. On the other hand, the synthesis and distillation of a volatile gas, methyl chloride, into the atmosphere could be a useful mechanism for disposing of excess chloride
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
this enzyme possibly functions in the control and regulation of the internal concentration of chloride ions in halophytic plant cells
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
kcat/KM for chloride is 19065fold lower than kcat/Km for iodide
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
the rate of production of methyl chloride is 270fold lower than production of methyl iodide
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
very low activity
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
-
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
the enzyme is responsible for the massive amounts of CH3Cl produced by this fungus
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
Vmax/Km for chloride is 709fold lower than Vmax/Km for iodide
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
production rate of chloromethane is 925fold lower than production rate of iodomethane
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
very low activity
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
recombinant protein methylates iodide with greater efficiency than chloride
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
recombinant proteins methylate iodide with greater efficiency than chloride
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
the enzyme is strictly dependent on S-adenosyl-L-methionine as a methyl donor
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
iodide is the preferred substrate
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
-
-
-
?
S-adenosyl-L-methionine + iodide
S-adenosyl-L-homocysteine + methyl iodide
-
iodide is the preferred substrate
-
-
?
additional information
?
-
a phylogenetic analysis with the HOL gene suggests that the ability to produce methyl halides is widespread among vascular plants. All wild-type plants strongly favor the methylation of I- to Br- to Cl-. Adult plants show a relative methylation preference ratio for I:Br:Cl of roughly 10000:50:1. Juvenile plants showed a ratio of roughly 40000:9:1
-
-
?
additional information
?
-
AtHOL1 is involved in glucosinolate metabolism and defense against phytopathogens. CH3Cl synthesized by AtHOL1 could be considered a byproduct of NCS- metabolism
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
purified enzyme is unable to use bisulfide (HS-) as an acceptor
-
-
?
additional information
?
-
-
purified enzyme is unable to use bisulfide (HS-) as an acceptor
-
-
?
additional information
?
-
-
also methylates HS to CH3SH (EC 2.1.1.9) at a rate comparable to that for iodide
-
-
?
additional information
?
-
-
the bifunctional enzyme also shows activity of EC 2.1.1.9
-
-
?
additional information
?
-
-
fluoride is not a substrate
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine. From the viewpoint of stratospheric ozone depletion, methyl bromide is the most destructive compound because it has a high ozone depletion potential
-
-
?
additional information
?
-
-
no activity with chloride, no activity with L-methionine, S-methyl methionine or dimethylsulfoniopropionate
-
-
?
additional information
?
-
-
the enzyme also catalyzes the methylation of HS- to methyl mercaptan (EC 2.1.1.9)
-
-
?
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
-
-
?
additional information
?
-
the enzyme also shows thiol methyltransferase activity (EC 2.1.1.9), high activity towards SCN-
-
-
?
additional information
?
-
-
bacteria contribute to iodine transfer from the terrestrial and marine ecosystems into the atmosphere
-
-
?
additional information
?
-
-
bacteria contribute to iodine transfer from the terrestrial and marine ecosystems into the atmosphere
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
additional information
?
-
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
an obvious function for a halophytic methylase would be the maintenance of homeostatic levels of cytoplasmic chloride ion. The secretion of excess chloride into the soil could not greatly benefit a halophytic plant. On the other hand, the synthesis and distillation of a volatile gas, methyl chloride, into the atmosphere could be a useful mechanism for disposing of excess chloride
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
this enzyme possibly functions in the control and regulation of the internal concentration of chloride ions in halophytic plant cells
-
-
?
S-adenosyl-L-methionine + chloride
S-adenosyl-L-homocysteine + methyl chloride
-
the enzyme is responsible for the massive amounts of CH3Cl produced by this fungus
-
-
?
additional information
?
-
a phylogenetic analysis with the HOL gene suggests that the ability to produce methyl halides is widespread among vascular plants. All wild-type plants strongly favor the methylation of I- to Br- to Cl-. Adult plants show a relative methylation preference ratio for I:Br:Cl of roughly 10000:50:1. Juvenile plants showed a ratio of roughly 40000:9:1
-
-
?
additional information
?
-
AtHOL1 is involved in glucosinolate metabolism and defense against phytopathogens. CH3Cl synthesized by AtHOL1 could be considered a byproduct of NCS- metabolism
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
the activation of AtHOL1, AtHOL2 and AtHOL3 genes contributes to the methyl halide emissions from Arabidopsis
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine. From the viewpoint of stratospheric ozone depletion, methyl bromide is the most destructive compound because it has a high ozone depletion potential
-
-
?
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
-
-
?
additional information
?
-
-
bacteria contribute to iodine transfer from the terrestrial and marine ecosystems into the atmosphere
-
-
?
additional information
?
-
-
bacteria contribute to iodine transfer from the terrestrial and marine ecosystems into the atmosphere
-
-
?
additional information
?
-
-
marine microalgae are the main oceanic source of methyl bromide. The monohalomethanes produced by marine microalgae are probably important in the global cycling of gaseous organohalogen species, especially bromine and iodine
-
-
?
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- 80°C, enzyme after the first gel filtration purification step, in 25 mM Tris acetate, pH 7.4, 10% glycerol, and 14 mM 2-mercaptoethanol, stable for over 2 months
-
-20°C to 4°C, partially purified enzyme, complete loss of activity overnight, also in the presence of protease inhibitors
-
-20°C, enzyme forms an aggregate with molecular mass of approximately 500000 Da
-20C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-20°C, purified protein stored in a buffer (140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 1 mM DTT, 30% glycerol), after 15 days, the recombinant protein AtHOL1 retains 40% of the iodide methyltransferase activity
-20°C, purified protein stored in a buffer (140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 1 mM DTT, 30% glycerol), after 15 days, the recombinant protein AtHOL1 retains 60% of the iodide methyltransferase activity
-20°C, purified protein stored in a buffer (140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 1 mM DTT, 30% glycerol), after 15 days, the recombinant protein AtHOL1 retains 90% of the iodide methyltransferase activity
-80°C, after affinity chromatography, the halide/bisulfide methyltransferase becomes extremely labile losing all activity after overnight storage
-
20°C, enzyme after the affinity chromatography purification step, 25 mM Tris acetate, pH 7.4, 14 mM 2-mercaptoethanol, and 30% glycerol, 12% remaining activity after 48 h
-
4°C, enzyme after anion exchange purification step, in 25 mM Tris acetate, pH 7.4, 14 mM 2-mercaptoethanol, and 175 mM NaCl, more than 70% remaining activity after 24 h and 55% after 48 h
-
4C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-20C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-
-20C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-
4C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-
4C, enzyme in cell extract is unstable and loses activities almost completely upon storage even if dithioerythritol, EDTA, protease inhibitor or glycerol are added to the extracts
-
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analysis
-
use of an MHT-expressing Escherichia coli to report on gene expression in a microbe within a moist soil under a range of growth conditions in a lab setting. The gas reporting approach is applied to monitor Escherichia coli conjugation within an agricultural soil and examine how hydration affects horizontal gene transfer
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
synthesis
-
producing methyl halides from non-food agricultural resources by using a symbiotic co-culture of an engineered yeast and the cellulolytic bacterium Actinotalea fermentans, methyl halide production from unprocessed switchgrass (Panicum virgatum), corn stover, sugar cane bagasse, and poplar (Populus sp.). Methyl halides are used as agricultural fumigants and are precursor molecules that can be catalytically converted to chemicals and fuels
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Saxena, D.; Aouad, S.; Attieh, J.; Saini, H.S.
Biochemical characterization of chloromethane emission from the wood-rotting fungus Phellinus pomaceus
Appl. Environ. Microbiol.
64
2831-2835
1998
Phellinus pomaceus
brenda
Rhew, R.C.; Ostergaard, L.; Saltzman, E.S.; Yanofsky, M.F.
Genetic control of methyl halide production in Arabidopsis
Curr. Biol.
13
1809-1813
2003
Arabidopsis thaliana (Q0WP12)
brenda
Attieh, J.M.; Hanson, A.D.; Saini, H.S.
Purification and characterization of a novel methyltransferase responsible for biosynthesis of halomethanes and methanethiol in Brassica oleracea
J. Biol. Chem.
270
9250-9257
1995
Brassica oleracea
brenda
Ni, X.; Hager, L.P.
cDNA cloning of Batis maritima methyl chloride transferase and purification of the enzyme
Proc. Natl. Acad. Sci. USA
95
12866-12871
1998
Batis maritima (Q9ZSZ7), Batis maritima
brenda
Ni, X.; Hager, L.P
Expression of Batis maritima methyl chloride transferase in Escherichia coli
Proc. Natl. Acad. Sci. USA
96
3611-3615
1999
Batis maritima (Q9ZSZ7), Batis maritima
brenda
Amachi, S.; Kamagata, Y.; Kanagawa, T.; Muramatsu, Y.
Bacteria mediate methylation of iodine in marine and terrestrial environments
Appl. Environ. Microbiol.
67
2718-2722
2001
Rhizobium sp., Rhizobium sp. MRCD 19
brenda
Ohsawa, N.; Tsujita, M.; Morikawa, S.; Itoh, N.
Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: halide ion methyltransferase from a marine microalga, Pavlova pinguis
Biosci. Biotechnol. Biochem.
65
2397-2404
2001
Pavlova pinguis
brenda
Itoh, N.; Toda, H.; Matsuda, M.; Negishi, T.; Taniguchi, T.; Ohsawa, N.
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)
BMC Plant Biol.
9
116
2009
Raphanus sativus (C6L2E7)
brenda
Bayer, T.S.; Widmaier, D.M.; Temme, K.; Mirsky, E.A.; Santi, D.V.; Voigt, C.A.
Synthesis of methyl halides from biomass using engineered microbes
J. Am. Chem. Soc.
131
6508-6515
2009
Brassica rapa, Burkholderia pseudomallei, Oryza sativa, Vitis vinifera, Paraburkholderia xenovorans, Burkholderia thailandensis, Paraburkholderia phytofirmans, Batis maritima
brenda
Nagatoshi Y, Nakamura T.
Arabidopsis HARMLESS TO OZONE LAYER protein methylates a glucosinolate breakdown product and functions in resistance to Pseudomonas syringae pv. maculicola
J. Biol. Chem.
284
19301-19309
2009
Arabidopsis thaliana (Q0WP12)
brenda
Itoh, N.; Tsujita, M.; Ando, T.; Hisatomi, G.; Higashi, T.
Formation and emission of monohalomethanes from marine algae
Phytochemistry
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