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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)

General Stability

General Stability on EC 1.7.1.1 - nitrate reductase (NADH)

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.03% SDS produces almost complete inactivation of NADH-diaphorase and NADH-nitrate reductase, while FNH2-nitrate reductase retains 60% of the original activity, FAD has no protecting effect
-
1 M guanidine hydrochloride, in presence of FAD, 80% inactivation of FNH2-nitrate reductase activity and NADH-nitrate reductase activity, NADH-diaphorase activity is unaffected
-
4 M urea, in presence of FAD, inactivation of FMNH2-nitrate reductase and NADH-nitrate reductase activity, only a slight effect on the NADH-diaphorase activity
-
dilution of a crude extract leads to increasing lability, much more stable in presence of both NADH and nitrate
-
enzyme in the crude extract is stable for several days at 0°C and for several months at -80°C
-
FAD protects from heat inactivation at 45°C
-
FAD stabilizes at 25°C, at 10°C FAD has no effect on stability
-
imposition of water stress or artificial extension of the dark period leads to significant reduction of nitrate reductase activity, but does not change in vitro nitrate reductase stability
-
inactivation by corn root proteinase, comparison of hydrolysis products
incubation of the native enzyme with either trypsin, Staphylococcus aureus V8 protease, or a natural inactivator protease from corn results in loss of NADH:nitrate reductase and NADH:cytochrome c reductase activity, but no loss of methyl viologen:nitrate reductase activity
-
leupeptin inhibits degradation of NADH-nitrate reductase by thiol-dependent acid endoproteinase in primary leaf extract
-
preincubation with NADH stabilizes activity at 0°C and at 25°C
presence of casein in phosphate buffer improves stability at 0°C but not at 30°C
-
stabilized at 0°C and at 30°C by buffer containing 0.25 M Tris-HCl, pH 8.5, 3 mM DTT, 0.005 mM FAD, 0.001 mM sodium molybdate and 1 mM EDTA
-
stabilized in vitro by addition of chymostatin to extraction buffer
-
the decay rate of nitrate reductase activity in crude extracts is due to spontaneous dissociation of the enzyme and to the effects of two decay factors, one present in the 0-30% and the other in the 50-70% saturated (NH4)2SO4 fraction of the crude extract
-
the enzyme is very susceptible to inactivation by maize root proteinase and trypsin
-