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Literature summary extracted from

  • Martinez-Espinosa, R.M.; Marhuenda-Egea, F.C.; Bonete, M.J.
    Assimilatory nitrate reductase from the haloarchaeon Haloferax mediterranei: Purification and characterization (2001), FEMS Microbiol. Lett., 204, 381-385.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.7.7.2 NaCl stabilizes, after 43 h, with 2.7 M, 2.1 M or 0.9 M NaCl: 95% loss of activity, after 90 h, with 4.3 M NaCl: completely stable Haloferax mediterranei

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.7.2 azide potent inhibitor, 79% loss of activity Haloferax mediterranei
1.7.7.2 cyanide almost complete inhibition Haloferax mediterranei
1.7.7.2 EDTA partial inhibition, 43% loss of activity Haloferax mediterranei
1.7.7.2 additional information not inhibited by potassium chlorate, dithiothreitol, p-hydroxymercuribenzoate, sulfite Haloferax mediterranei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.7.2 0.066
-
 reduced methyl viologen
-
 Haloferax mediterranei
1.7.7.2 0.95
-
 nitrate
-
 Haloferax mediterranei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.7.2 iron-sulfur centre enzyme contains Fe-S clusters Haloferax mediterranei
1.7.7.2 NaCl activity depends on salt concentration Haloferax mediterranei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.7.2 50000
-
 1 * 105000 + 1 * 50000, SDS-PAGE Haloferax mediterranei
1.7.7.2 105000
-
 1 * 105000 + 1 * 50000, SDS-PAGE Haloferax mediterranei
1.7.7.2 132000
-
 gel filtration Haloferax mediterranei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.7.2 nitrate + reduced ferredoxin Haloferax mediterranei assimilatory nitrate reduction nitrite + oxidized ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.7.2 Haloferax mediterranei
-
 extreme halophilic archaeon
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.7.2 177fold purification Haloferax mediterranei

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.7.2 0.55
-
-
 Haloferax mediterranei

Storage Stability

EC Number Storage Stability Organism
1.7.7.2 4°C, 50 mM phosphate buffer, pH 7, 20% glycerol, 2 weeks, no loss of activity Haloferax mediterranei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.7.2 additional information not as electron donors: NADH, NADPH, dithionite, 8% of maximum activity with 1mM FADH2 and less than 7% of maximum activity with 1 mM reduced 2,6-dichlorophenolindophenol or phenazine methosulfate Haloferax mediterranei ?
-
 ?
1.7.7.2 nitrate + reduced ferredoxin 100 nM dithionite reduced ferredoxin with 94% of the activity with reduced methyl viologen Haloferax mediterranei nitrite + H2O + oxidized ferredoxin
-
 ?
1.7.7.2 nitrate + reduced ferredoxin assimilatory nitrate reduction Haloferax mediterranei nitrite + oxidized ferredoxin
-
 ?
1.7.7.2 nitrate + reduced methyl viologen reduced methyl viologen is the best electron donor in vitro Haloferax mediterranei nitrite + oxidized methyl viologen
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.7.2 dimer 1 * 105000 + 1 * 50000, SDS-PAGE Haloferax mediterranei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.7.2 additional information
-
 strong dependence of activity on the temperature and NaCl concentrations Haloferax mediterranei
1.7.7.2 60
-
 for NaCl concentrations of 1.3 and 0.9 M Haloferax mediterranei
1.7.7.2 80
-
 for NaCl concentrations of 3.1 and 2.2 M Haloferax mediterranei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.7.2 9
-
-
 Haloferax mediterranei

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.7.2 iron-sulfur centre enzyme contains Fe-S clusters Haloferax mediterranei
1.7.7.2 additional information no FAD or cytochromes are observed Haloferax mediterranei