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Literature summary for 1.7.1.1 extracted from

  • Quinn, G.B.; Trimboli, A.J.; Prosser, I.M.; Barber, M.J.
    Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:nitrate reductase (1996), Arch. Biochem. Biophys., 327, 151-160.
    View publication on PubMed
Search for more literature for 1.7.1.1

Cloned(Commentary)

Cloned (Comment) Organism
the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in Escherichia coli Spinacia oleracea

Inhibitors

Inhibitors Comment Organism Structure
adenine inhibition of the recombinant FAD domain Spinacia oleracea
adenosine inhibition of the recombinant FAD domain Spinacia oleracea
adenosine 5'-diphosphoribose inhibition of the recombinant FAD domain Spinacia oleracea
ADP inhibition of the recombinant FAD domain Spinacia oleracea
AMP inhibition of the recombinant FAD domain Spinacia oleracea
ferricyanide inhibition of the recombinant FAD domain Spinacia oleracea
NAD+ inhibition of the recombinant FAD domain Spinacia oleracea
nicotinamide inhibition of the recombinant FAD domain Spinacia oleracea
NMN inhibition of the recombinant FAD domain Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values of the the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in E. coli Spinacia oleracea
0.017
-
 NADH recombinant FAD domain Spinacia oleracea
0.034
-
 ferricyanide recombinant FAD domain Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in E. coli show a MW of 30000 Da by SDS-PAGE Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the C-terminal 268 residues corresponding to the flavin-containing domain, amplified and expressed in Escherichia coli Spinacia oleracea

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the isolated flavin-containing domain is capable of reducing cytochrome b5 directly Spinacia oleracea ?
-
 ?
nitrate + NADH
-
 Spinacia oleracea nitrite + NAD+ + H2O
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Spinacia oleracea

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.2
-
 ADP inhibition of the recombinant FAD domain Spinacia oleracea
0.2
-
 ADPribose inhibition of the recombinant FAD domain Spinacia oleracea
0.6
-
 AMP inhibition of the recombinant FAD domain Spinacia oleracea
1.9
-
 NAD+ inhibition of the recombinant FAD domain Spinacia oleracea
4.8
-
 adenosine inhibition of the recombinant FAD domain Spinacia oleracea
23
-
 ferricyanide inhibition of the recombinant FAD domain Spinacia oleracea
26
-
 adenine inhibition of the recombinant FAD domain Spinacia oleracea
62
-
 NMN inhibition of the recombinant FAD domain Spinacia oleracea
122
-
 nicotinamide inhibition of the recombinant FAD domain Spinacia oleracea