ExplorEnz: EC 6.1.1.26

Your query returned 1 entry. Printable version

6.1.1.26

Accepted name:

pyrrolysine—tRNA^Pyl ligase

Reaction:

ATP + L-pyrrolysine + tRNA^Pyl = AMP + diphosphate + L-pyrrolysyl-tRNA^Pyl

Glossary:

pyrrolysine = N⁶-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]-L-lysine

Other name(s):

PylS; pyrrolysyl-tRNA synthetase

Systematic name:

L-pyrrolysine:tRNA^Pyl ligase (AMP-forming)

Comments:

In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNA^Pyl, with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl—tRNA ligase. The enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids [1].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	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. Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo. Nature 431 (2004) 333–335. [DOI] [PMID: 15329732]
2.	Polycarpo, C., Ambrogelly, A., Bérubé, A., Winbush, S.M., McCloskey, J.A., Crain, P.F., Wood, J.L. and Söll, D. An aminoacyl-tRNA synthetase that specifically activates pyrrolysine. Proc. Natl. Acad. Sci. USA 101 (2004) 12450–12454. [DOI] [PMID: 15314242]
3.	Schimmel, P. and Beebe, K. Molecular biology: genetic code seizes pyrrolysine. Nature 431 (2004) 257–258. [DOI] [PMID: 15372017]

[EC 6.1.1.26 created 2007]