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Literature summary for 1.7.1.1 extracted from

  • Barber, M.J.; Desai, S.K.; Marohnic, C.C.
    Assimilatory nitrate reductase: lysine 741 participates in pyridine nucleotide binding via charge complementarity (2001), Arch. Biochem. Biophys., 394, 99-110.
    View publication on PubMed
Search for more literature for 1.7.1.1

Protein Variants

Protein Variants Comment Organism
K714A functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741E functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741H functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741M functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741P functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741Q functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea
K741R functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order Spinacia oleracea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrate + NADH Spinacia oleracea the enzyme catalyzes the regulated and rate-limiting step in the utilization of inorganic nitrogen by higher plants nitrite + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes K741R, K741H, K714A, K741E, K741M, K741Q, K741P Spinacia oleracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Spinacia oleracea 2 ferrocyanide + NAD+ + H+
-
 ?
nitrate + NADH
-
 Spinacia oleracea nitrite + NAD+ + H2O
-
 ?
nitrate + NADH the enzyme catalyzes the regulated and rate-limiting step in the utilization of inorganic nitrogen by higher plants Spinacia oleracea nitrite + NAD+ + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Spinacia oleracea