Methyl halide transferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.1.1.165 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Methyl halide transferase (EC 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.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
This enzyme contributes to the methyl halide emissions from Arabidopsis thaliana.
Chloride transfer
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.[7] 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),[2] red algae (Endocladia muricata), and the ice plant (Mesembryanthemum crystallinum), each of which is a known CH3Cl producer.[7][8]
References
- ↑ Ni, X.; Hager, L.P. (1999). "Expression of Batis maritima methyl chloride transferase in Escherichia coli". Proc. Natl. Acad. Sci. USA. 96 (7): 3611–3615. Bibcode:1999PNAS...96.3611N. doi:10.1073/pnas.96.7.3611. PMC 22342. PMID 10097085.
- 1 2 Saxena, D.; Aouad, S.; Attieh, J.; Saini, H.S. (1998). "Biochemical characterization of chloromethane emission from the wood-rotting fungus Phellinus pomaceus". Appl. Environ. Microbiol. 64 (8): 2831–2835. Bibcode:1998ApEnM..64.2831S. doi:10.1128/AEM.64.8.2831-2835.1998. PMC 106779. PMID 9687437.
- ↑ Attieh, J.M.; Hanson, A.D.; Saini, H.S. (1995). "Purification and characterization of a novel methyltransferase responsible for biosynthesis of halomethanes and methanethiol in Brassica oleracea". J. Biol. Chem. 270 (16): 9250–9257. doi:10.1074/jbc.270.16.9250. PMID 7721844.
- ↑ Itoh, N.; Toda, H.; Matsuda, M.; Negishi, T.; Taniguchi, T.; Ohsawa, N. (2009). "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. doi:10.1186/1471-2229-9-116. PMC 2752461. PMID 19723322.
- ↑ Ohsawa, N.; Tsujita, M.; Morikawa, S.; Itoh, N. (2001). "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 (11): 2397–2404. doi:10.1271/bbb.65.2397. PMID 11791711.
- ↑ Nagatoshi, Y.; Nakamura, T. (2007). "Characterization of three halide methyltransferases in Arabidopsis thaliana". Plant Biotechnol. 24 (5): 503–506. doi:10.5511/plantbiotechnology.24.503.
- 1 2 Ni X, Hager LP; Purification of the Enzyme (1998). "cDNA Cloning of Batis maritima Methyl Chloride Transferase". Proc Natl Acad Sci USA. 95 (22): 12866–71. doi:10.1073/pnas.95.22.12866. PMC 23635. PMID 9789006.
- ↑ Ni X, Hager LP (1999). "Expression of Batis maritima Methyl Chloride Transferase in Escherichia coli". Proc Natl Acad Sci USA. 96 (7): 3611–5. Bibcode:1999PNAS...96.3611N. doi:10.1073/pnas.96.7.3611. PMC 22342. PMID 10097085.
External links
- Methyl+halide+transferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)