1.9.6.1: nitrate reductase (cytochrome)

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

Reaction

2 ferrocytochrome + 2 H+ +

Synonyms

benzyl viologen-nitrate reductase, EC 1.7.99.4, mmol_1648, More, NAP, NAP enzyme, Nap-alpha, NAP-beta, NapA, napA-beta, NapAB, NapABC, NapDAGHB, NapEDABC, nitrate reductase, periplasmic, periplasmic nitrate reductase, periplasmic nitrate reductases, reductase, nitrate (cytochrome), respiratory nitrate reductase, single subunit Nap-type periplasmic nitrate reductase

ECTree

     1 Oxidoreductases

         1.9 Acting on a heme group of donors

             1.9.6 With a nitrogenous group as acceptor

                1.9.6.1 nitrate reductase (cytochrome)

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Results	in table
1	Activating Compound
4555	AA Sequence
1	Application
1	CAS Registry Number
20	Cloned(Commentary)
94	Cofactor
5	Crystallization (Commentary)
5	Expression
66	General Information
1	General Stability
27	Inhibitors
4	kcat/KM [mM/s]
14	KM Value [mM]
53	Localization
50	Metals/Ions
17	Molecular Weight [Da]
37	Natural Substrates/ Products (Substrates)
140	Organism
4	Pathway
2	PDB ID
6	pH Optimum
2	pH Range
2	Posttranslational Modification
13	Protein Variants
7	Purification (Commentary)
21	Reaction
3	Reaction Type
89	Reference
3	Source Tissue
4	Specific Activity [micromol/min/mg]
2	Storage Stability
91	Substrates and Products (Substrate)
31	Subunits
261	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
3	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.9.6.1 - nitrate reductase (cytochrome)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

homology modeling of structure, the substrate channel and catalytic pocket are more basic than other NapA proteins, which may influence the substrate binding as well as product release

Campylobacter jejuni

Q5HV12

764685

sitting-drop vapour-diffusion method, crystals of the oxidized form of this enzyme are obtained using polyethylene glycol 3350 as precipitant. A single crystal diffracted to beyond 1.5 A at the ESRF (ID14-1), which is the highest resolution reported to date for a nitrate reductase. The unit-cell parameters are a = 142.2, b = 82.4, c = 96.8 A, beta = 100.7°, space group C2, and one heterodimer is present per asymmetric unit

Cupriavidus necator H16

-

695337

X-ray diffraction structure analysis, resolution 2.2 A, PDB ID 2jio, modelling

Desulfovibrio desulfuricans

P81186

742648

purified recombinant NapDNHis/NapA complex, small angle X-ray scattering analysis, modelling

Escherichia coli

P33937

742486

vapor diffusion method

Escherichia coli

-

674891