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Literature summary extracted from

  • Yamaguchi, K.; Shuta, K.; Suzuki, S.
    Roles of Trp144 and Tyr203 in copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013 (2005), Biochem. Biophys. Res. Commun., 336, 210-214.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.1 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
1.7.2.1 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
1.7.2.1 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

EC Number Organism UniProt Comment Textmining
1.7.2.1 Achromobacter cycloclastes
-
 IAM1013
-
1.7.2.1 Achromobacter cycloclastes IAM1013
-
 IAM1013
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 nitrite + reduced benzyl viologen
-
 Achromobacter cycloclastes NO + H2O + oxidized benzyl viologen
-
 ?
1.7.2.1 nitrite + reduced benzyl viologen
-
 Achromobacter cycloclastes IAM1013 NO + H2O + oxidized benzyl viologen
-
 ?
1.7.2.1 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
-
 ?
1.7.2.1 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

EC Number Synonyms Comment Organism
1.7.2.1 AcNIR
-
 Achromobacter cycloclastes

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.1 additional information
-
 additional information
-
 Achromobacter cycloclastes