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Literature summary for 1.7.1.3 extracted from

  • Ringel, P.; Krausze, J.; Van Heuvel, J.; Curth, U.; Pierik, A.; Herzog, S.; Mendel, R.; Kruse, T.
    Biochemical characterization of molybdenum cofactor-free nitrate reductase from Neurospora crassa (2013), J. Biol. Chem., 288, 14657-14671.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.29
-
 nitrate pH 7.2, temperature not specified in the publication Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa P08619
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.24
-
 pH 7.2, temperature not specified in the publication Neurospora crassa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + NADPH + H+
-
 Neurospora crassa nitrite + NADP+
-
 ?

Subunits

Subunits Comment Organism
dimer in presence of molybdenum cofactor, enzyme forms a dimer, gel filtration, sedimentation velocity analysis Neurospora crassa

Synonyms

Synonyms Comment Organism
nit-3
-
 Neurospora crassa

Cofactor

Cofactor Comment Organism Structure
FAD involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place Neurospora crassa
heme involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place Neurospora crassa
molybdenum cofactor cofactor is necessary and sufficient to induce dimer formation. The molybdenum center of nitrate reductase reconstituted in vitro from apo-enzyme and cofactor shows an EPR spectrum identical to holo-enzyme. Insertion of this cofactor into the enzyme occurs independent from the insertion of any other NR redox cofactor Neurospora crassa
NADPH
-
 Neurospora crassa