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
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Reaction
Reaction on EC 1.7.1.3 - nitrate reductase (NADPH)
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nitrite + NADP+ + H2O = nitrate + NADPH + H+
multicenter redox enzyme. Ser920, Arg921 and Arg932 are suggested to be the key enzymes to investigate for a role in determining pyridine nucleotide specificity. Arg932 may be playing a role in binding the adenine ring of NADPH
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nitrite + NADP+ + H2O = nitrate + NADPH + H+
random order rapid-equilibrium mechanism, two functional parts: 1. heat labile, FAD and haemoprotein containing, binds NADPH and transfers electrons from NADPH via FAD and perhaps cytochrome b to acceptors such as cytochrome c, 2. heat stable, molybdenum containing, accepts electrons from reduced viologen dyes and transfers them to nitrate
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nitrite + NADP+ + H2O = nitrate + NADPH + H+
sulfhydryl groups may participate in the binding of the protein subunits
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