1.7.1.3: nitrate reductase (NADPH)
This is an abbreviated version!
For detailed information about nitrate reductase (NADPH), go to the full flat file.
Word Map on EC 1.7.1.3
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1.7.1.3
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neurospora
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crassa
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nidulans
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molybdenum
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molybdenum-containing
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nadph-cytochrome
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molybdopterin
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positive-acting
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pathway-specific
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viologen-nitrate
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reductase-deficient
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nitrogen-related
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tungstate
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nadh:nitrate
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synthesis
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analysis
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medicine
- 1.7.1.3
- neurospora
- crassa
- nidulans
- molybdenum
-
molybdenum-containing
-
nadph-cytochrome
- molybdopterin
-
positive-acting
-
pathway-specific
-
viologen-nitrate
-
reductase-deficient
-
nitrogen-related
- tungstate
-
nadh:nitrate
- synthesis
- analysis
- medicine
Reaction
Synonyms
assimilatory NADPH-nitrate reductase, assimilatory NADPH:nitrate reductase, Assimilatory nitrate reductase, assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase, EC 1.6.6.3, EC 1.7.99.4, MSMEG_2837, NADPH-dependent nitrate reductase, NADPH-nitrate reductase, NADPH2:nitrate oxidoreductase, NADPH:nitrate reductase, NADPH:NR, NaR1, narB, nit-3, nitrate reductase, nitrate reductase (NADPH), nitrate reductase (reduced nicotinamide adenine dinucleotide phosphate), nitrate reductase [NADPH], NR, triphosphopyridine nucleotide-nitrate reductase
ECTree
1.7.1.3 nitrate reductase (NADPH)Advanced search results
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results (Engineering
Engineering on EC 1.7.1.3 - nitrate reductase (NADPH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H654A/H677A
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site-directed mutagenesis, CD spectroscopy shows no negative effects of the introduced mutations on protein secondary structure in comparison to the wild-type protein, but the mutant contains no heme, while the FAD binding ability is not significantly disturbed
R778E
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site-directed mutagenesis, an FAD-binding mutant. The mutant binds essentially the same amount of Moco as does the wild type protein
R921S
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little impact on NADPH and NADH activity, no importance for pyridine nucleotide specificity
R921T
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little impact on NADPH and NADH activity, no importance for pyridine nucleotide specificity
R932Q
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1/4 wild type NADPH activity is retained, twice as much NADH activity is present as compared to wild type
R932S
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1/10 wild type NADPH activity is retained, 2/3 of wild type NADH activity
S920D
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important for the enzyme's interaction with the pyridine nucleotide substrates. Mutant retains ~2% of the NADPH activity of the wild type while it has an increased NADH activity, ~15% higher. It is concluded that Ser920 is a ligand involved in binding the 2' phosphate of NADPH in the wild type enzyme
S920D/R932S
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greatest decrease in NADPH activity of all created mutants, shows that Arg932 is a residue interacting with the pyridine nucleotide coenzyme electron donors and that Ser920 and Arg932 have effects on substrate binding and catalytic activity. Both residues may be ligands to the 2' phosphate of NADPH in the wild type cyt b reductase fragment of nitrate reductase
additional information
additional information
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studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes
additional information
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different structural gene (niaD) and cofactor gene (cnx) mutants are analyzed concerning their flavin and molybdenum content
additional information
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studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes
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additional information
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the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview
additional information
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the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview
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additional information
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nit-1 mutant: lacks all activities except FAD-dependent NADPH:cytochrome c reductase activity,nit-2 mutant: reduced FAD:- and reduced methyl viologen:nitrate reductase activities but lacks the other two activities
additional information
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nit-3 mutant (FGSC 262): reduced FAD-nitrate reductase and reduced methylviologen-nitrate reductase activities
additional information
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nit-1 mutant, suggested to produce the complete apoenzyme
additional information
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several mutations of recombinant cyt b reductase fragment of nitrate reductase in the region Ser920, Arg921 and Arg932 are created. Conversion from NADPH-specific to virtually NADH-specific cyt b reductase fragment of nitrate reductase
