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Literature summary extracted from

  • Prudencio, M.; Eady, R.R.; Sawers, G.
    Catalytic and spectroscopic analysis of blue copper-containing nitrite reductase mutants altered in the environment of the type 2 copper centre: implications for substrate interaction (2001), Biochem. J., 353, 259-266.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.1 D92E and D92N mutant enzyme Achromobacter xylosoxidans

Protein Variants

EC Number Protein Variants Comment Organism
1.7.2.1 D92E mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 20-30% of wild-type activity with physiological electron donor azurin I Achromobacter xylosoxidans
1.7.2.1 D92N mutation in type 2 Cu center, very low activity with artificial electron donors methyl viologen and sodium dithionite, 60-70% of wild-type activity with physiological electron donor azurin I Achromobacter xylosoxidans
1.7.2.1 H139A mutation in type 1 Cu center, very low activity with the artificial electron donor methyl viologen, no activity with the physiological electron donor azurin I Achromobacter xylosoxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 copper the type 1 Cu center functions as electron acceptor from the physiological electron donor azurin I, the type 2 Cu center is involved in binding and reduction of the substrate Achromobacter xylosoxidans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.1 reduced azurin + O2 Achromobacter xylosoxidans putative physiological electron donor oxidized azurin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Achromobacter xylosoxidans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1 recombinant wild-type and D92E and D92N mutant enzyme Achromobacter xylosoxidans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.1 45.2
-
 native recombinant enzyme, azurin Achromobacter xylosoxidans
1.7.2.1 107
-
 native recombinant enzyme, dithionite Achromobacter xylosoxidans
1.7.2.1 168
-
 native recombinant enzyme, methyl viologen Achromobacter xylosoxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 nitrite + ferrocytochrome c
-
 Achromobacter xylosoxidans nitric oxide + H2O + ferricytochrome c
-
 ?
1.7.2.1 NO2- + reduced azurin putative physiological electron donor Achromobacter xylosoxidans NO + oxidized azurin
-
 ?
1.7.2.1 reduced azurin + O2 putative physiological electron donor Achromobacter xylosoxidans oxidized azurin + H2O
-
 ?