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Literature summary for 2.1.1.182 extracted from
- The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit (2006), Arch. Biochem. Biophys., 449, 57-63.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| protein S21 | S21 probably inhibits KsgA activity in an indirect way, presumably by stabilizing 30S in a conformation that for whatever reason cannot be methylated by KsgA | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA | recombinant KsgA is able to efficiently methylate 30S subunits isolated from strains of Escherichia coli resistant to kasugamycin, but not wild-type 30S subunits, indicating that the methylation function is specific for A1518 and A1519. KsgA is unable to utilize 30S subunits in the translationally active state as a substrate | Escherichia coli | 4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| KsgA | - |
Escherichia coli |
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Release 2023.1 (January 2023)
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