Methyl halide transferase

Methyl halide transferase
Identifiers
EC number 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

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

S-adenosyl-L-methionine + iodide S-adenosyl-L-homocysteine + methyl iodide

This enzyme contributes to the methyl halide emissions from Arabidopsis thaliana.

Chlorine too

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

  1. ↑ 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. doi:10.1073/pnas.96.7.3611. PMC 22342Freely accessible. PMID 10097085.
  2. 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. PMC 106779Freely accessible. PMID 9687437.
  3. ↑ 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.
  4. ↑ 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: 116–116. doi:10.1186/1471-2229-9-116. PMC 2752461Freely accessible. PMID 19723322.
  5. ↑ 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.
  6. ↑ Nagatoshi, Y.; Nakamura, T. (2007). "Characterization of three halide methyltransferases in Arabidopsis thaliana". Plant Biotechnol. 24: 503–506. doi:10.5511/plantbiotechnology.24.503.
  7. 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 23635Freely accessible. PMID 9789006.
  8. ↑ Ni X, Hager LP (1999). "Expression of Batis maritima Methyl Chloride Transferase in Escherichia coli". Proc Natl Acad Sci USA. 96 (7): 3611–5. doi:10.1073/pnas.96.7.3611. PMC 22342Freely accessible. PMID 10097085.
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