Pyrrolysine—tRNAPyl ligase
| Pyrrolysine—tRNAPyl ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.1.1.26 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Pyrrolysine—tRNAPyl ligase (EC 6.1.1.26, PylS, pyrrolysyl-tRNA synthetase) is an enzyme with systematic name L-pyrrolysine:tRNAPyl ligase (AMP-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + L-pyrrolysine + tRNAPyl AMP + diphosphate + L-pyrrolysyl-tRNAPyl
This enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids.
References
- ^ Blight, S.K., Larue, R.C., Mahapatra, A., Longstaff, D.G., Chang, E., Zhao, G., Kang, P.T., Green-Church, K.B., Chan, M.K. and Krzycki, J.A. (2004). "Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo". Nature. 431: 333–335. doi:10.1038/nature02895. PMID 15329732.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Polycarpo, C., Ambrogelly, A., Bérubé, A., Winbush, S.M., McCloskey, J.A., Crain, P.F., Wood, J.L. and Söll, D. (2004). "An aminoacyl-tRNA synthetase that specifically activates pyrrolysine". Proc. Natl. Acad. Sci. USA. 101: 12450–12454. doi:10.1073/pnas.0405362101. PMC 515082. PMID 15314242.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Schimmel, P. and Beebe, K. (2004). "Molecular biology: genetic code seizes pyrrolysine". Nature. 431: 257–258. doi:10.1038/431257a. PMID 15372017.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Pyrrolysine---tRNAPyl+ligase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)