EC 6.1.1.26 - Pyrrolysine—tRNAPyl ligase

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IntEnz Enzyme Nomenclature
EC 6.1.1.26

Names

Accepted name:
pyrrolysine—tRNAPyl ligase
Other names:
PylS
pyrrolysyl-tRNA synthetase
PylRS
Systematic name:
L-pyrrolysine:tRNAPyl ligase (AMP-forming)

Reaction

Comments:

In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNAPyl, 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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

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 tRNACUA with pyrrolysine in vitro and in vivo.
    Nature 431: 333-335 (2004). [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: 12450-12454 (2004). [PMID: 15314242]
  3. Schimmel, P. and Beebe, K.
    Molecular biology: genetic code seizes pyrrolysine.
    Nature 431: 257-258 (2004). [PMID: 15372017]

[EC 6.1.1.26 created 2007]