Pyrrolysine—tRNAPyl ligase
| Pyrrolysine—tRNAPyl ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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.; Krzycki, J.A. (2004). "Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo". Nature. 431: 333–335. PMID 15329732. doi:10.1038/nature02895.
- ↑ Polycarpo, C.; Ambrogelly, A.; Gonzalès, A.; Winbush, S.M.; McCloskey, J.A.; Crain, P.F.; Wood, J.L.; Söll, D. (2004). "An aminoacyl-tRNA synthetase that specifically activates pyrrolysine". Proc. Natl. Acad. Sci. USA. 101: 12450–12454. PMC 515082
. PMID 15314242. doi:10.1073/pnas.0405362101. - ↑ Schimmel, P.; Beebe, K. (2004). "Molecular biology: genetic code seizes pyrrolysine". Nature. 431: 257–258. PMID 15372017. doi:10.1038/431257a.
External links
- Pyrrolysine---tRNAPyl ligase at the US National Library of Medicine Medical Subject Headings (MeSH)
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