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Literature summary for 2.1.1.9 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Raphanus sativus |
| expressed in Escherichia coli BL21(DE3) cells | Raphanus sativus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.04 | - |
thiocyanate | pH 7.0, 30°C, purified recombinant enzyme | Raphanus sativus |  |
| 0.04 | - |
thiocyanate | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
| 0.19 | - |
S-adenosyl-L-methionine | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
| 4.47 | - |
Iodide | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
| 12.24 | - |
SH- | pH 7.0, 30°C, purified recombinant enzyme | Raphanus sativus | |
| 12.24 | - |
bisulfide | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
| 177.3 | - |
bromide | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
| 1657 | - |
chloride | in 20 mM MES (pH 7.0), at 30°C | Raphanus sativus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27500 | - |
calculated from amino acid sequence | Raphanus sativus |
| 29000 | - |
SDS-PAGE | Raphanus sativus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Raphanus sativus | C6L2E7 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| DEAE-Toyopearl 650 M column chromatography and Ni-Sepharose column chromatography | Raphanus sativus |
| partial | Raphanus sativus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Raphanus sativus | - |
| leaf | highest activity in mature leaves | Raphanus sativus | - |
| additional information | no activity in mature roots | Raphanus sativus | - |
| stem | - |
Raphanus sativus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| bisulfide + S-adenosyl-L-methionine | highest activity | Raphanus sativus | methanethiol + S-adenosyl-L-homocysteine | - |
? | |
| 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 | ? | - |
? | |
| additional information | the enzyme also shows halide methyltransferase activity | Raphanus sativus | ? | - |
? | |
| additional information | the enzyme shows no activity towards CN- | Raphanus sativus | ? | - |
? | |
| S-adenosyl-L-methionine + bromide | - |
Raphanus sativus | S-adenosyl-L-homocysteine + bromomethane | - |
? | |
| S-adenosyl-L-methionine + chloride | very low activity | Raphanus sativus | S-adenosyl-L-homocysteine + chloromethane | - |
? | |
| S-adenosyl-L-methionine + HS- | - |
Raphanus sativus | ? | - |
? | |
| S-adenosyl-L-methionine + iodide | - |
Raphanus sativus | S-adenosyl-L-homocysteine + iodomethane | - |
? | |
| thiocyanate + S-adenosyl-L-methionine | - |
Raphanus sativus | ? | - |
? | |
| thiocyanate + S-adenosyl-L-methionine | - |
Raphanus sativus | methyl thiocyanate + S-adenosyl-L-homocysteine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 29000, SDS-PAGE | Raphanus sativus |
| ? | x * 27500, calculated from sequence | Raphanus sativus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HMT/HTMT | - |
Raphanus sativus |
| HTMT | - |
Raphanus sativus |
| S-adenosylmethionine-dependent halide/thiol methyltransferase | - |
Raphanus sativus |
| S-adenosylmethionine-dependent halide/thiol methyltransferase | bifunctional enzyme | Raphanus sativus |
| TMT | - |
Raphanus sativus |
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