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Literature summary for 6.1.1.26 extracted from

  • Heinemann, I.U.; ODonoghue, P.; Madinger, C.; Benner, J.; Randau, L.; Noren, C.J.; Soell, D.
    The appearance of pyrrolysine in tRNAHis guanylyltransferase by neutral evolution (2009), Proc. Natl. Acad. Sci. USA, 106, 21103-21108.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Methanosarcina acetivorans
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-pyrrolysine + tRNAPyl the Methanosarcina acetivorans tRNAhis guanylyltranferase Thg1 gene contains an in-frame TAG codon. Its presence in Methanosarcina mRNA may lead to pyrrolysine incorporation achieved by Pyl-tRNAPyl, the product of pyrrolysyl-tRNA synthetase. Translation of Thg1 mRNA leads to a full-length, Pyl-containing, active enzyme as determined by immunoblotting, mass spectrometry, and biochemical analysis Methanosarcina acetivorans AMP + diphosphate + L-pyrrolysyl-tRNAPyl
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General Information

General Information Comment Organism
physiological function pyrrolysine insertion is akin to natural suppression and unlike the active stop codon reassignment that is required for selenocysteine insertion. In Thg1, pyrrolysine is a dispensable residue that appears to confer no selective advantage Methanosarcina acetivorans