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1.7.1.1: nitrate reductase (NADH)

This is an abbreviated version!
For detailed information about nitrate reductase (NADH), go to the full flat file.

Word Map on EC 1.7.1.1

Reaction

nitrite
+
NAD+
+
H2O
=
nitrate
+
NADH
+
H+

Synonyms

assimilatory NADH:nitrate reductase, Assimilatory nitrate reductase, cytosolic NADH nitrate reductase, EC 1.6.6.1, EC 1.7.99.4, MSMEG_4206, MSMEI_4108, NADH-dependent nitrate reductase, NADH-Nar, NADH-nitrate reductase, NADH-NO3- reductase, NADH:nitrate oxidoreductase, NaR, NaR1, NasA, NasC, NIA1, Nia2, nitrate reductase, NR, NR1, NR2, Pden_4449, reductase, nitrate

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.1 With NAD+ or NADP+ as acceptor
                1.7.1.1 nitrate reductase (NADH)

Engineering

Engineering on EC 1.7.1.1 - nitrate reductase (NADH)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C191A
-
enzyme is still produced, but it is inactive
C191S
-
enzyme is still produced, but it is inactive
S266A
-
48% of the activity of wild-type enzyme
S534A
-
the mutant is not inhibited by 14-3-3 proteins
S521D
C17S
-
visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain
C240A
-
decrease of diaphorase activity
C240G
-
decrease of diaphorase activity
C240S
-
decrease of diaphorase activity, thermal stability is slightly decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -219 mV compared to -268 mV in the wild-type domain
C54S
-
visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain,the oxidation reduction midpoint potential for the FAD/FADH2 couple is -197 mV compared to -268 mV in the wild-type domain
C62S
-
visible and CD spectra are very similar to that of the wild-type domain, thermal stability is decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -226 mV compared to -268 mV in the wild-type domain
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
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
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
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
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
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
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
additional information