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Literature summary for 2.1.1.165 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)

Cloned (Comment) Organism
expressed in Escherichia coli Raphanus sativus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.19
-
S-adenosyl-L-methionine pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
4.47
-
Iodide pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
177.3
-
bromide pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus
1657
-
chloride pH 7.0, 30°C, purified recombinant enzyme Raphanus sativus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
27500
-
x * 27500, calculated from sequence Raphanus sativus
29000
-
x * 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
partial Raphanus sativus

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Raphanus sativus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 thiol methyltransferase activity (EC 2.1.1.9), high activity towards SCN- Raphanus sativus ?
-
?
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
-
?
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
-
?
S-adenosyl-L-methionine + iodide iodide is the preferred substrate Raphanus sativus S-adenosyl-L-homocysteine + methyl iodide
-
?

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 bifunctional enzyme Raphanus sativus