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Literature summary for 2.8.4.4 extracted from

  • Molle, T.; Moreau, Y.; Clemancey, M.; Forouhar, F.; Ravanat, J.L.; Duraffourg, N.; Fourmond, V.; Latour, J.M.; Gambarelli, S.; Mulliez, E.; Atta, M.
    Redox behavior of the S-adenosylmethionine (SAM)-binding Fe-S cluster in methylthiotransferase RimO, toward understanding dual SAM activity (2016), Biochemistry, 55, 5798-5808.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor Thermotoga maritima
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3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
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?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X2H6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor
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Thermotoga maritima 3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor
-
?

Synonyms

Synonyms Comment Organism
RimO
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Thermotoga maritima

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Thermotoga maritima
[4Fe-4S]-center contains two iron-sulfur clusters Thermotoga maritima