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Literature summary extracted from

  • Esclapez, J.; Zafrilla, B.; Martínez-Espinosa, R.M.; Bonete, M.J.
    Cu-NirK from Haloferax mediterranei as an example of metalloprotein maturation and exportation via Tat system (2013), Biochim. Biophys. Acta, 1834, 1003-1009.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.1 expression in Haloferax volcanii, intracellular enzyme Haloferax mediterranei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.1 0.41
-
 reduced methyl viologen pH and temperature not specified in the publication Haloferax mediterranei
1.7.2.1 4.04
-
 nitrite pH and temperature not specified in the publication Haloferax mediterranei

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.2.1 cytoplasm important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system Haloferax mediterranei 5737
-
1.7.2.1 extracellular important differences in the primary structure of the cytoplasmic enzyme form and the extracellularv enzyme form, indicating that Haloferax mediterranei could carry out a maturation and exportation process within the cell before the protein is exported to the S-layer. Several conserved signals found in Cu-NirK from Haloferax mediterranei sequence indicate that these processes are closely related to the Tat system Haloferax mediterranei
-
-
1.7.2.1 membrane
-
 Haloferax mediterranei 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.1 KCl optimum salt concentration: 2 M Haloferax mediterranei
1.7.2.1 NaCl optimum salt concentration: 2 M Haloferax mediterranei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.1 39800
-
 3 * 39800, SDS-PAGE, intracellular enzyme Haloferax mediterranei
1.7.2.1 44300
-
 3 * 44300, SDS-PAGE, extracellular enzyme Haloferax mediterranei
1.7.2.1 103000
-
 gel filtration, intracellular enzyme Haloferax mediterranei

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Haloferax mediterranei D0RAY2
-
-
1.7.2.1 Haloferax mediterranei DSM 1411 D0RAY2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1
-
 Haloferax mediterranei

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.7.2.1 culture medium
-
 Haloferax mediterranei
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 nitrite + reduced methyl viologen
-
 Haloferax mediterranei NO + oxidized methyl viologen + H2O
-
 ?
1.7.2.1 nitrite + reduced methyl viologen
-
 Haloferax mediterranei DSM 1411 NO + oxidized methyl viologen + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.1 trimer 3 * 39800, SDS-PAGE, intracellular enzyme Haloferax mediterranei
1.7.2.1 trimer 3 * 44300, SDS-PAGE, extracellular enzyme Haloferax mediterranei

Synonyms

EC Number Synonyms Comment Organism
1.7.2.1 Cu-NirK
-
 Haloferax mediterranei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.1 70
-
-
 Haloferax mediterranei