EC Number | Cloned (Comment) | Organism |
---|---|---|
1.7.2.4 | expressed in Escherichia coli | Achromobacter cycloclastes |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.7.2.4 | Cu | Cu is bound by apo NosL, a coexpressed protein which is necessary for the assembling process of nitrous oxide reductase | Achromobacter cycloclastes |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.7.2.4 | Achromobacter cycloclastes | - |
- |
- |
4.99.1.2 | Achromobacter cycloclastes | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.7.2.4 | DEAE-FF ion exchange chromatography and Resource Q column chromatography | Achromobacter cycloclastes |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.99.1.2 | RHg+ + H+ | - |
Achromobacter cycloclastes | RH + Hg2+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.99.1.2 | More | MerB has a high structural similarity to the copper binding protein NosL, MerB and apo NosL are the only members of a new structural superfamily, each containing two perpendicularly arranged bbab motifs | Achromobacter cycloclastes |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.7.2.4 | N2OR | - |
Achromobacter cycloclastes |
1.7.2.4 | nitrous oxide reductase | - |
Achromobacter cycloclastes |
4.99.1.2 | alkylmercury mercuric-lyase | - |
Achromobacter cycloclastes |
4.99.1.2 | merB | - |
Achromobacter cycloclastes |