Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC

Accepted Name
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase.
Alternative Name(s)
tRNA-yW synthesizing enzyme-2.
Reaction catalysed
S-adenosyl-L-methionine + 4-demethylwyosine(37) in tRNA(Phe) <=> S-methyl-5'-thioadenosine + 7-((3S)-3-amino-3-carboxypropyl)-4-demethylwyosine(37) in tRNA(Phe)
  • The enzyme, which is found in all eukaryotes and in the majority of Euryarchaeota (but not in the Crenarchaeota), is involved in the hypermodification of the guanine nucleoside at position 37 of tRNA leading to formation of assorted wye bases.
  • This modification is essential for translational reading-frame maintenance.
  • The eukaryotic enzyme is involved in biosynthesis of the tricyclic base wybutosine, which is found only in tRNA(Phe).
PRIAM enzyme-specific profiles2.5.1.114
KEGG Ligand Database for Enzyme Nomenclature2.5.1.114
IUBMB Enzyme Nomenclature2.5.1.114
MEDLINEFind literature relating to
Q8W4K1, TYW23_ARATH;  Q8H4D4, TYW23_ORYSJ;  Q58D65, TYW2_BOVIN;  
Q0P466, TYW2_DANRE;  Q53H54, TYW2_HUMAN;  Q4R3U8, TYW2_MACFA;  
Q58952, TYW2_METJA;  Q8BG71, TYW2_MOUSE;  O58523, TYW2_PYRHO;  
Q4V8B8, TYW2_RAT;  Q09832, TYW2_SCHPO;  Q04235, TYW2_YEAST;  

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.5.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-