Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.7.1.1 extracted from

  • Barber, M.J.; Desai, S.K.; Marohnic, C.C.; Hernandez, H.H.; Pollock, V.V.
    Synthesis and bacterial expression of a gene encoding the heme domain of assimilatory nitrate reductase (2002), Arch. Biochem. Biophys., 402, 38-50.
    View publication on PubMed
Search for more literature for 1.7.1.1

Protein Variants

Protein Variants Comment Organism
additional information expression of fragment A542-Y647 in Escherichia coli, production of enzyme heme domain evidenced by pink cells. Reconstitution of –NADH:cytochrome c reductase activity in presence of recombinant form of spinach nitrate reductase flavin domain Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Spinacia oleracea 2 ferrocyanide + NAD+ + H+
-
 ?
2 ferricytochrome c + NADH
-
 Spinacia oleracea 2 ferrocytochrome c + NAD+ + H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4
-
 NADH
-
 Spinacia oleracea
1.5
-
 ferricytochrome c pH 7.0, 25°C, functional FAD-containing domain plus heme-containig domain Spinacia oleracea
1300
-
 ferricyanide pH 7.0, 25°C, functional FAD-containing domain Spinacia oleracea
1400
-
 NADH pH 7.0, 25°C, functional FAD-containing domain domain plus heme-containig domain Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Spinacia oleracea
NADH
-
 Spinacia oleracea