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Literature summary extracted from

  • Kathirvelu, V.; Perche-Letuvee, P.; Latour, J.; Atta, M.; Forouhar, F.; Gambarelli, S.; Garcia-Serres, R.
    Spectroscopic evidence for cofactor-substrate interaction in the radical-SAM enzyme TYW1 (2017), Dalton Trans., 46, 13211-13219 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.44 N1-methylguanine37 in tRNAPhe + pyruvate + S-adenosyl-L-methionine Methanocaldococcus jannaschii
-
 4-demethylwyosine37 in tRNAPhe + L-methionine + 5'-deoxyadenosine + CO2 + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.44 Methanocaldococcus jannaschii Q57705
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.44 N1-methylguanine37 in tRNAPhe + pyruvate + S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii 4-demethylwyosine37 in tRNAPhe + L-methionine + 5'-deoxyadenosine + CO2 + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.3.44 TYW1
-
 Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.3.44 S-adenosyl-L-methionine
-
 Methanocaldococcus jannaschii
4.1.3.44 [4Fe-4S]-center contains two [4Fe-4S] clusters Methanocaldococcus jannaschii