Literature summary for 1.7.2.1 extracted from

Prudencio, M.; Eady, R.R.; Sawers, G.
The blue copper-containing nitrite reductase from Alcaligenes xylosoxidans: cloning of the nirA gene and characterization of the recombinant enzyme (1999), J. Bacteriol., 181, 2323-2329.

Search for more literature for 1.7.2.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Achromobacter xylosoxidans

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.035	-	NO2-	-	Achromobacter xylosoxidans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	blue copper enzyme that shows little absorbance in the 460 nm range, purified recombinant nonactivated enzyme contains 1.97 mol Copper/mol enzyme, the CuSO4 activated enzyme contains 5.97 mol copper/mol enzyme i.e. 6 copper atoms per trimer, CuSO4 activation restores type 2 copper centers which are the sites of catalysis	Achromobacter xylosoxidans

Organism

Organism	UniProt	Comment	Textmining
Achromobacter xylosoxidans	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Achromobacter xylosoxidans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
10.8	-	recombinant enzyme, without activation, enzyme has only type 1 copper centers	Achromobacter xylosoxidans
167.7	-	recombinant enzyme, after activation with CuSO4	Achromobacter xylosoxidans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrite + ferrocytochrome c	-	Achromobacter xylosoxidans	nitric oxide + H2O + ferricytochrome c	-	?

Subunits

Subunits	Comment	Organism
trimer	recombinant enzyme	Achromobacter xylosoxidans

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
80	-	native and purified enzyme retain 50% activity after 20 min exposure	Achromobacter xylosoxidans

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Release 2023.1 (January 2023)