TRNA wybutosine-synthesizing protein 3
| tRNA wybutosine-synthesizing protein 3 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The enzyme as folded by AlphaFold | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.1.282 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
tRNA wybutosine-synthesizing protein 3, known also as tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase, abbreviated to TYW3 is an S-adenosyl-L-methionine-dependent methyltransferase that is involved in the biosynthetic pathway of wybutosine, a hyper-modified guanosine possessing tricyclic base found at the 3'-position which is close to the anticodon of eukaryotic phenylalanine tRNA.[1] TYW3 is believed to also methylate the carboxyl group of leucine to form α-leucine esters.[2] The enzyme catalyzes the following reaction,
- 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) + S-adenosyl-L-homocysteine + H+
The modifications this enzyme makes are important for translational reading-frame maintenance. TYW3 is found in all eukaryotes and in some archaea, but not in bacteria.[3][4]
References
- ^ "tRNA-yW synthesizing protein 3 homolog [ Homo sapiens (human) ]". NIH. Protein Databases. 7 April 2025. Retrieved 26 April 2025.
- ^ "P53177 · TYW3_YEAST". UniProt. Database. 2025. Retrieved 26 April 2025.
- ^ "ENZYME entry: EC 2.1.1.282". Expasy. 2025. Retrieved 26 April 2025.
- ^ "TRNA ENZYME EC NUM". KEGG. Database. 2025. Retrieved 26 April 2025.