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Literature summary extracted from

  • Jacques, J.G.; Burlat, B.; Arnoux, P.; Sabaty, M.; Guigliarelli, B.; Leger, C.; Pignol, D.; Fourmond, V.
    Kinetics of substrate inhibition of periplasmic nitrate reductase (2014), Biochim. Biophys. Acta, 1837, 1801-1809 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.9.6.1 nitrate at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.9.6.1 additional information
-
 additional information steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle Cereibacter sphaeroides

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.9.6.1 periplasm
-
 Cereibacter sphaeroides
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.9.6.1 Molybdenum within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.9.6.1 2 ferrocytochrome + 2 H+ + nitrate Cereibacter sphaeroides
-
 2 ferricytochrome + nitrite
-
 ?
1.9.6.1 2 ferrocytochrome + 2 H+ + nitrate Cereibacter sphaeroides DSM 158
-
 2 ferricytochrome + nitrite
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.9.6.1 Cereibacter sphaeroides Q53176
-
-
1.9.6.1 Cereibacter sphaeroides DSM 158 Q53176
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.9.6.1 2 ferrocytochrome + 2 H+ + nitrate
-
 Cereibacter sphaeroides 2 ferricytochrome + nitrite
-
 ?
1.9.6.1 2 ferrocytochrome + 2 H+ + nitrate
-
 Cereibacter sphaeroides DSM 158 2 ferricytochrome + nitrite
-
 ?
1.9.6.1 additional information the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation Cereibacter sphaeroides ?
-
 ?
1.9.6.1 additional information the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation Cereibacter sphaeroides DSM 158 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.9.6.1 heterodimer
-
 Cereibacter sphaeroides

Synonyms

EC Number Synonyms Comment Organism
1.9.6.1 NapA
-
 Cereibacter sphaeroides
1.9.6.1 periplasmic nitrate reductase
-
 Cereibacter sphaeroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.9.6.1 25
-
 assay at Cereibacter sphaeroides

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.9.6.1 6
-
 assay at Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
1.9.6.1 cytochrome c two surface-exposed c-type hemes, NapB Cereibacter sphaeroides
1.9.6.1 molybdenum cofactor i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview Cereibacter sphaeroides
1.9.6.1 [4Fe-4S] cluster in close proximity to the MoCo Cereibacter sphaeroides

General Information

EC Number General Information Comment Organism
1.9.6.1 evolution the enzyme belongs to the DMSO reductase family Cereibacter sphaeroides