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Literature summary extracted from
- Investigating the intermediates in the reaction of ribonucleoside triphosphate reductase from Lactobacillus leichmannii: An application of HF EPR-RFQ technology (2011), J. Magn. Reson., 213, 32-45.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.17.4.2 | analysis | development of a rapid freeze-quench apparatus for the preparation of millisecond quench time rapid freeze-quench samples which can be packed into small sample tubes used for continuous-wave and pulsed high-frequency electron paramagnetic resonance spectroscopy | Lactobacillus leichmannii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.4.2 | Lactobacillus leichmannii | Q59490 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.4.2 | adenosylcobalamin-dependent ribonucleoside-triphosphate reductase | - |
Lactobacillus leichmannii |
| 1.17.4.2 | RTPR | - |
Lactobacillus leichmannii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.17.4.2 | adenosylcobalamin | in the course of catalysis, the protein active site presents the reacting molecules with an environment that includes a hydrogen bond to the thiyl radical and intervening residues or solvent mediating an exchange coupling between the thiyl radical and cob(II)alamin | Lactobacillus leichmannii |  |
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Release 2023.1 (January 2023)
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