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Literature summary for 2.1.1.9 extracted from

  • Ohsawa, N.; Tsujita, M.; Morikawa, S.; Itoh, N.
    Purification and characterization of a monohalomethane-producing enzyme S-adenosyl-L-methionine: halide ion methyltransferase from a marine microalga, Pavlova pinguis (2001), Biosci. Biotechnol. Biochem., 65, 2397-2404.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Pavlova pinguis
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the bifunctional enzyme also catalyzes the methylation of iodide and to a lesser extent bromide and chloride Pavlova pinguis ?
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?
S-adenosyl-L-methionine + HS- the enzyme is strictly dependent on S-adenosyl-L-methionine as a methyl donor Pavlova pinguis S-adenosyl-L-homocysteine + CH3SH
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?

Synonyms

Synonyms Comment Organism
HMT
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Pavlova pinguis