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Literature summary for 1.7.2.1 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)

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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
-
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
-
-
membrane
-
Haloferax mediterranei 16020
-

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei D0RAY2
-
-
Haloferax mediterranei DSM 1411 D0RAY2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Haloferax mediterranei

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
Haloferax mediterranei
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
Cu-NirK
-
Haloferax mediterranei

Temperature Optimum [°C]

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