Protein Variants | Comment | Organism |
---|---|---|
W144L | visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods | Achromobacter cycloclastes |
W144L/Y203L | visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods | Achromobacter cycloclastes |
Y203L | visible absorption and EPR spectrum is similar to that of wild-type AcNIR. The redox potentials of the mutant is also nearly equal to that of wild-type. Although the enzymatic activities of the mutants are also the same as that of wild-type enzyme, the intermolecular electron transfer rate constants from pseudoazurin to mutant AcNIRs is 3-4fold less than that from pseudoazurin to wild-type AcNIR using electrochemical methods | Achromobacter cycloclastes |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Achromobacter cycloclastes | - |
IAM1013 | - |
Achromobacter cycloclastes IAM1013 | - |
IAM1013 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + reduced benzyl viologen | - |
Achromobacter cycloclastes | NO + H2O + oxidized benzyl viologen | - |
? | |
nitrite + reduced benzyl viologen | - |
Achromobacter cycloclastes IAM1013 | NO + H2O + oxidized benzyl viologen | - |
? | |
nitrite + reduced pseudoazurin | the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system | Achromobacter cycloclastes | NO + oxidized pseudoazurin | - |
? | |
nitrite + reduced pseudoazurin | the rate-determining step in the enzyme reaction sequence is not the intermolecular electron transfer process between pseudoazurin and AcNIR, but the reduction of substrate by AcNIR in the steady-state assay system | Achromobacter cycloclastes IAM1013 | NO + oxidized pseudoazurin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AcNIR | - |
Achromobacter cycloclastes |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Achromobacter cycloclastes |