Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.3.44 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)

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

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q57705
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
TYW1
-
Methanocaldococcus jannaschii

Cofactor

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