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Literature summary for 6.5.1.3 extracted from
- The structural basis of ribozyme-catalyzed RNA assembly (2007), Science, 315, 1549-1553.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 2.6 A crystal structure | Enterobacteria phage L1 |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Enterobacteria phage L1 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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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Release 2023.1 (January 2023)
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