Crystallization (Comment) | Organism |
---|---|
modified form of the enzyme that contains an additional covalent bond between residues Tyr303 and Gln360 in complex with phosphate to 1.45 A resolution, and with sulfite to 1.8 A resolution, structure of unmodified enzyme in complex with nitrite to 1.83 A resolution. Structure reveal the presence of a covalent bond between the CE2 atom of the catalytic Tyr303 and the S atom of Cys305, which might be responsible for the higher nitrite reductase activity. The formation of the second covalent bond by Tyr303 leads to a decrease in both the nitrite and sulfite reductase activities of the enzyme. Tyr303 is located at the exit from the putative proton-transport channel to the active site | Thioalkalivibrio nitratireducens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thioalkalivibrio nitratireducens | Q5F2I3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + reduced methyl viologen | - |
Thioalkalivibrio nitratireducens | NH3 + oxidized methyl viologen + H2O | - |
? | |
sulfite + reduced methyl viologen | - |
Thioalkalivibrio nitratireducens | H2S + oxidized methyl viologen + H2O | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.023 | - |
sulfite | modified enzyme that contains an additional covalent bond between residues Tyr303 and Gln360, pH 7.0, 20°C | Thioalkalivibrio nitratireducens | |
0.039 | - |
sulfite | unmodified enzyme, pH 7.0, 20°C | Thioalkalivibrio nitratireducens | |
1195 | - |
nitrite | modified enzyme that contains an additional covalent bond between residues Tyr303 and Gln360, pH 7.0, 20°C | Thioalkalivibrio nitratireducens | |
2860 | - |
nitrite | unmodified enzyme, pH 7.0, 20°C | Thioalkalivibrio nitratireducens |