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Literature summary extracted from

  • Robertson, M.P.; Scott, W.G.
    The structural basis of ribozyme-catalyzed RNA assembly (2007), Science, 315, 1549-1553.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.3 2.6 A crystal structure Enterobacteria phage L1

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.5.1.3 Mg2+ L1 ligase is an obligate metalloenzyme that is highly specific for Mg2+. It is selected in the presence of 60 mM MgCl2 and functions optimally in Mg2+ concentrations as high as 100 mM Enterobacteria phage L1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m Enterobacteria phage L1 the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond AMP + diphosphate + (ribonucleotide)n+m
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Organism

EC Number Organism UniProt Comment Textmining
6.5.1.3 Enterobacteria phage L1
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.3 ATP + (ribonucleotide)n + (ribonucleotide)m the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond Enterobacteria phage L1 AMP + diphosphate + (ribonucleotide)n+m
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 ?