Literature summary for 1.7.2.1 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.

Search for more literature for 1.7.2.1

Protein Variants

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

Organism	UniProt	Comment	Textmining
Achromobacter cycloclastes	-	IAM1013	-
Achromobacter cycloclastes IAM1013	-	IAM1013	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
AcNIR	-	Achromobacter cycloclastes

Turnover Number [1/s]

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)