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Methyl halide transferase

Methyl halide transferase
Identifiers
EC no.2.1.1.165
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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.

Chloride transfer

Main article: 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.[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. Bibcode:1999PNAS...96.3611N. doi:10.1073/pnas.96.7.3611. PMC 22342. PMID 10097085.
  2. ^ a b 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.
  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. doi:10.1186/1471-2229-9-116. PMC 2752461. 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 (5): 503–506. doi:10.5511/plantbiotechnology.24.503.
  7. ^ a b 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.
  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. Bibcode:1999PNAS...96.3611N. doi:10.1073/pnas.96.7.3611. PMC 22342. PMID 10097085.
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