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Literature summary extracted from

  • 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) (2009), BMC Plant Biol., 9, 116.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.9 expressed in Escherichia coli Raphanus sativus
2.1.1.9 expressed in Escherichia coli BL21(DE3) cells Raphanus sativus
2.1.1.165 expressed in Escherichia coli Raphanus sativus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.9 0.04
-
 thiocyanate pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
2.1.1.9 0.04
-
 thiocyanate in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.9 0.19
-
 S-adenosyl-L-methionine in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.9 4.47
-
 Iodide in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.9 12.24
-
 SH- pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
2.1.1.9 12.24
-
 bisulfide in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.9 177.3
-
 bromide in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.9 1657
-
 chloride in 20 mM MES (pH 7.0), at 30°C Raphanus sativus
2.1.1.165 0.19
-
 S-adenosyl-L-methionine pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
2.1.1.165 4.47
-
 Iodide pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
2.1.1.165 177.3
-
 bromide pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
2.1.1.165 1657
-
 chloride pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.9 27500
-
 calculated from amino acid sequence Raphanus sativus
2.1.1.9 29000
-
 SDS-PAGE Raphanus sativus
2.1.1.165 27500
-
 x * 27500, calculated from sequence Raphanus sativus
2.1.1.165 29000
-
 x * 29000, SDS-PAGE Raphanus sativus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.9 additional information Raphanus sativus 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 ?
-
 ?
2.1.1.165 additional information Raphanus sativus 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.9 Raphanus sativus C6L2E7
-
-
2.1.1.165 Raphanus sativus C6L2E7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.9 DEAE-Toyopearl 650 M column chromatography and Ni-Sepharose column chromatography Raphanus sativus
2.1.1.9 partial Raphanus sativus
2.1.1.165 partial Raphanus sativus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.9 leaf
-
 Raphanus sativus
-
2.1.1.9 leaf highest activity in mature leaves Raphanus sativus
-
2.1.1.9 additional information no activity in mature roots Raphanus sativus
-
2.1.1.9 stem
-
 Raphanus sativus
-
2.1.1.165 leaf
-
 Raphanus sativus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.9 bisulfide + S-adenosyl-L-methionine highest activity Raphanus sativus methanethiol + S-adenosyl-L-homocysteine
-
 ?
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 Raphanus sativus ?
-
 ?
2.1.1.9 additional information the enzyme also shows halide methyltransferase activity Raphanus sativus ?
-
 ?
2.1.1.9 additional information the enzyme shows no activity towards CN- Raphanus sativus ?
-
 ?
2.1.1.9 S-adenosyl-L-methionine + bromide
-
 Raphanus sativus S-adenosyl-L-homocysteine + bromomethane
-
 ?
2.1.1.9 S-adenosyl-L-methionine + chloride very low activity Raphanus sativus S-adenosyl-L-homocysteine + chloromethane
-
 ?
2.1.1.9 S-adenosyl-L-methionine + HS-
-
 Raphanus sativus ?
-
 ?
2.1.1.9 S-adenosyl-L-methionine + iodide
-
 Raphanus sativus S-adenosyl-L-homocysteine + iodomethane
-
 ?
2.1.1.9 thiocyanate + S-adenosyl-L-methionine
-
 Raphanus sativus ?
-
 ?
2.1.1.9 thiocyanate + S-adenosyl-L-methionine
-
 Raphanus sativus methyl thiocyanate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.165 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 Raphanus sativus ?
-
 ?
2.1.1.165 additional information the enzyme also shows thiol methyltransferase activity (EC 2.1.1.9), high activity towards SCN- Raphanus sativus ?
-
 ?
2.1.1.165 S-adenosyl-L-methionine + bromide production rate of bromomethane is 24fold lower than production rate of iodomethane Raphanus sativus S-adenosyl-L-homocysteine + methyl bromide
-
 ?
2.1.1.165 S-adenosyl-L-methionine + chloride production rate of chloromethane is 925fold lower than production rate of iodomethane Raphanus sativus S-adenosyl-L-homocysteine + methyl chloride
-
 ?
2.1.1.165 S-adenosyl-L-methionine + iodide iodide is the preferred substrate Raphanus sativus S-adenosyl-L-homocysteine + methyl iodide
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.9 ? x * 29000, SDS-PAGE Raphanus sativus
2.1.1.9 ? x * 27500, calculated from sequence Raphanus sativus
2.1.1.165 ? x * 29000, SDS-PAGE Raphanus sativus
2.1.1.165 ? x * 27500, calculated from sequence Raphanus sativus

Synonyms

EC Number Synonyms Comment Organism
2.1.1.9 HMT/HTMT
-
 Raphanus sativus
2.1.1.9 HTMT
-
 Raphanus sativus
2.1.1.9 S-adenosylmethionine-dependent halide/thiol methyltransferase
-
 Raphanus sativus
2.1.1.9 S-adenosylmethionine-dependent halide/thiol methyltransferase bifunctional enzyme Raphanus sativus
2.1.1.9 TMT
-
 Raphanus sativus
2.1.1.165 HMT/HTMT
-
 Raphanus sativus
2.1.1.165 HTMT
-
 Raphanus sativus
2.1.1.165 S-adenosylmethionine-dependent halide/thiol methyltransferase bifunctional enzyme Raphanus sativus