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Literature summary extracted from

  • Yousafzai, F.K.; Eady, R.R.
    Dithionite reduction kinetics of the dissimilatory copper-containing nitrite reductase of Alcalegenes xylosoxidans. The SO2.- radical binds to the substrate binding type 2 copper site before the type 2 copper is reduced (2002), J. Biol. Chem., 277, 34067-34073.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.1 0.036
-
 nitrite
-
 Achromobacter xylosoxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 copper enzyme contains type 1 and type 2 copper centers, 6.3 copper atoms per trimer, blue copper enzyme Achromobacter xylosoxidans

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1
-
 Achromobacter xylosoxidans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.1 236
-
-
 Achromobacter xylosoxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 nitrite + dithionite type 1 copper of the fully loaded protein is reduced both directly by dithionite and indirectly by the type 2 copper site via intramolecular electron transfer Achromobacter xylosoxidans NO + reduced dithionite
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.1 trimer
-
 Achromobacter xylosoxidans

Synonyms

EC Number Synonyms Comment Organism
1.7.2.1 AxNiR
-
 Achromobacter xylosoxidans