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Literature summary extracted from
- NrdH-redoxin protein mediates high enzyme activity in manganese-reconstituted ribonucleotide reductase from Bacillus anthracis (2011), J. Biol. Chem., 286, 33053-33060.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.17.4.1 | 79800 | - |
subunit NrdE, SDS-PAGE and calculated | Bacillus anthracis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.17.4.1 | Bacillus anthracis | Q81G56 | - |
- |
| 1.17.4.1 | Bacillus anthracis ATCC 14579 | Q81G56 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.17.4.1 | NrdE | - |
Bacillus anthracis |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.17.4.1 | physiological function | the properties of tyrosyl radical metalloprotein NrdF loaded with iron or manganese are in general similar for interaction with catalyitc subunit NrdE and flavodoxin protein NrdI. The enzyme activity in presence of manganese is approximately an order of magnitude higher than that in presence of iron in the presence of the class specific physiological reductant NrdH | Bacillus anthracis |
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Release 2023.1 (January 2023)
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