Entry |
|
Name |
pyrrolysine---tRNAPyl ligase;
PylS;
pyrrolysyl-tRNA synthetase
|
Class |
Ligases;
Forming carbon-oxygen bonds;
Ligases forming aminoacyl-tRNA and related compounds
|
Sysname |
L-pyrrolysine:tRNAPyl ligase (AMP-forming)
|
Reaction(IUBMB) |
ATP + L-pyrrolysine + tRNAPyl = AMP + diphosphate + L-pyrrolysyl-tRNAPyl [RN: R08578]
|
Reaction(KEGG) |
|
Substrate |
|
Product |
|
Comment |
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].
|
History |
EC 6.1.1.26 created 2007
|
Pathway |
ec00970 | Aminoacyl-tRNA biosynthesis |
|
Orthology |
K11627 | pyrrolysyl-tRNA synthetase |
|
Genes |
» show all
|
Reference |
|
Authors |
Blight SK, Larue RC, Mahapatra A, Longstaff DG, Chang E, Zhao G, Kang PT, Green-Church KB, Chan MK, Krzycki JA. |
Title |
Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo. |
Journal |
|
Sequence |
|
Reference |
|
Authors |
Polycarpo C, Ambrogelly A, Berube A, Winbush SM, McCloskey JA, Crain PF, Wood JL, Soll D |
Title |
An aminoacyl-tRNA synthetase that specifically activates pyrrolysine. |
Journal |
|
Sequence |
|
Reference |
|
Authors |
Schimmel P, Beebe K. |
Title |
Molecular biology: genetic code seizes pyrrolysine. |
Journal |
|
Other DBs |
ExplorEnz - The Enzyme Database: | 6.1.1.26 |
ExPASy - ENZYME nomenclature database: | 6.1.1.26 |
|
LinkDB |
|