Methyl halide transferase
{{Infobox enzyme
| Name = Methyl halide transferase
| EC_number = 2.1.1.165
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Methyl halide transferase ({{EC number|2.1.1.165}}, MCT, methyl chloride transferase, S-adenosyl-L-methionine:halide/bisulfide methyltransferase, AtHOL1, AtHOL2, AtHOL3, HMT, S-adenosyl-L-methionine: halide ion methyltransferase, SAM:halide ion methyltransferase) is an enzyme with systematic name S-adenosylmethionine:iodide methyltransferase.{{cite journal | title = Expression of Batis maritima methyl chloride transferase in Escherichia coli |author1 = Ni, X. |author2 =Hager, L.P. |journal = Proc. Natl. Acad. Sci. USA |date = 1999 |volume = 96 |pages = 3611–3615 |pmid = 10097085 | doi = 10.1073/pnas.96.7.3611 | issue = 7 | pmc = 22342|bibcode = 1999PNAS...96.3611N |doi-access = free }}{{cite journal | title = Biochemical characterization of chloromethane emission from the wood-rotting fungus Phellinus pomaceus |author1 = Saxena, D. |author2 =Aouad, S. |author3 =Attieh, J. |author4 =Saini, H.S. |journal = Appl. Environ. Microbiol. |date = 1998 |volume = 64 |pages = 2831–2835 |pmid = 9687437 | issue = 8 |doi = 10.1128/AEM.64.8.2831-2835.1998 | pmc = 106779|bibcode = 1998ApEnM..64.2831S }}{{cite journal | title = Purification and characterization of a novel methyltransferase responsible for biosynthesis of halomethanes and methanethiol in Brassica oleracea |author1 = Attieh, J.M. |author2 =Hanson, A.D. |author3 =Saini, H.S. |journal = J. Biol. Chem. |date = 1995 |volume = 270 |pages = 9250–9257 |pmid = 7721844 | doi = 10.1074/jbc.270.16.9250 | issue = 16|doi-access = free }}{{cite journal | title = 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) |author1 = Itoh, N. |author2 =Toda, H. |author3 =Matsuda, M. |author4 =Negishi, T. |author5 =Taniguchi, T. |author6 =Ohsawa, N. | journal = BMC Plant Biol. |date = 2009 |volume = 9 |pages = 116 |pmid = 19723322 | doi = 10.1186/1471-2229-9-116 | pmc = 2752461 |doi-access = free }}{{cite journal | title = Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: halide ion methyltransferase from a marine microalga, Pavlova pinguis |author1 = Ohsawa, N. |author2 =Tsujita, M. |author3 =Morikawa, S. |author4 =Itoh, N. |journal = Biosci. Biotechnol. Biochem. |date = 2001 |volume = 65 |pages = 2397–2404 |pmid = 11791711 | doi = 10.1271/bbb.65.2397 | issue = 11|doi-access = free }}{{cite journal | title = Characterization of three halide methyltransferases in Arabidopsis thaliana |author1 = Nagatoshi, Y. |author2 = Nakamura, T. |journal = Plant Biotechnol. |date = 2007 |volume = 24 |issue = 5 |pages = 503–506 |doi=10.5511/plantbiotechnology.24.503|doi-access = free }} This enzyme catalyses the following chemical reaction
: S-adenosyl-L-methionine + iodide S-adenosyl-L-homocysteine + methyl iodide
This enzyme contributes to the methyl halide emissions from Arabidopsis thaliana.
Chloride transfer
{{main|Chloromethane#Biogenesis}}
The salt marsh plant Batis maritima contains the enzyme methyl chloride transferase that catalyzes the synthesis of chloromethane (CH3Cl) from S-adenosine-L-methionine and chloride.{{cite journal |author1 = Ni X, Hager LP | year = 1998 | title = cDNA Cloning of Batis maritima Methyl Chloride Transferase |author2 = Purification of the Enzyme | journal = Proc Natl Acad Sci USA | volume = 95 | pages = 12866–71 | doi = 10.1073/pnas.95.22.12866 | pmid = 9789006 | issue = 22 | pmc = 23635| doi-access = free }} This protein has been purified and expressed in E. coli, and seems to be present in other organisms such as white rot fungi (Phellinus pomaceus), red algae (Endocladia muricata), and the ice plant (Mesembryanthemum crystallinum), each of which is a known CH3Cl producer.{{cite journal |vauthors=Ni X, Hager LP | year = 1999 | title = Expression of Batis maritima Methyl Chloride Transferase in Escherichia coli | journal = Proc Natl Acad Sci USA | volume = 96 | pages = 3611–5 | doi = 10.1073/pnas.96.7.3611 | pmid = 10097085 | issue = 7 | pmc = 22342| bibcode = 1999PNAS...96.3611N | doi-access = free }}
References
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External links
- {{MeshName|Methyl+halide+transferase}}
{{One carbon transferases}}
{{Enzymes}}
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