BRENDA - Enzyme Database
show all sequences of 1.9.6.1

Periplasmic nitrate reductases and formate dehydrogenases biological control of the chemical properties of Mo and W for fine tuning of reactivity, substrate specificity and metabolic role

Gonzalez, P.; Rivas, M.; Mota, C.; Brondino, C.; Moura, I.; Moura, J.; Coord. Chem. Rev. 257, 315-331 (2013)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene nap and nap gene cluster, genetic organization and sequence comparisons
Anaeromyxobacter dehalogenans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Bradyrhizobium japonicum
gene nap and nap gene cluster, genetic organization and sequence comparisons
Campylobacter jejuni subsp. jejuni
gene nap and nap gene cluster, genetic organization and sequence comparisons
Cupriavidus necator
gene nap and nap gene cluster, genetic organization and sequence comparisons
Desulfitobacterium hafniense
gene nap and nap gene cluster, genetic organization and sequence comparisons
Desulfovibrio desulfuricans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Escherichia coli
gene nap and nap gene cluster, genetic organization and sequence comparisons
Paracoccus denitrificans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Paracoccus pantotrophus
gene nap and nap gene cluster, genetic organization and sequence comparisons
Pseudomonas sp.
gene nap and nap gene cluster, genetic organization and sequence comparisons
Rhodobacter sphaeroides
gene nap and nap gene cluster, genetic organization and sequence comparisons
Shewanella gelidimarina
gene nap and nap gene cluster, genetic organization and sequence comparisons
Shewanella oneidensis
gene nap and nap gene cluster, genetic organization and sequence comparisons
Wolinella succinogenes
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Anaeromyxobacter dehalogenans
-
-
periplasm
-
Campylobacter jejuni subsp. jejuni
-
-
periplasm
-
Cupriavidus necator
-
-
periplasm
-
Desulfitobacterium hafniense
-
-
periplasm
-
Escherichia coli
-
-
periplasm
-
Paracoccus denitrificans
-
-
periplasm
-
Paracoccus pantotrophus
-
-
periplasm
-
Pseudomonas sp.
-
-
periplasm
-
Rhodobacter sphaeroides
-
-
periplasm
-
Shewanella gelidimarina
-
-
periplasm
-
Shewanella oneidensis
-
-
periplasm
-
Wolinella succinogenes
-
-
periplasm
-
Bradyrhizobium japonicum
-
-
periplasm
-
Desulfovibrio desulfuricans
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
in the heme/cytochrome cofactor
Anaeromyxobacter dehalogenans
Fe2+
in the heme/cytochrome cofactor
Bradyrhizobium japonicum
Fe2+
in the heme/cytochrome cofactor
Campylobacter jejuni subsp. jejuni
Fe2+
in the heme/cytochrome cofactor
Cupriavidus necator
Fe2+
in the heme/cytochrome cofactor
Desulfitobacterium hafniense
Fe2+
in the heme/cytochrome cofactor
Escherichia coli
Fe2+
in the heme/cytochrome cofactor
Paracoccus denitrificans
Fe2+
in the heme/cytochrome cofactor
Paracoccus pantotrophus
Fe2+
in the heme/cytochrome cofactor
Pseudomonas sp.
Fe2+
in the heme/cytochrome cofactor
Rhodobacter sphaeroides
Fe2+
in the heme/cytochrome cofactor
Shewanella gelidimarina
Fe2+
in the heme/cytochrome cofactor
Shewanella oneidensis
Fe2+
in the heme/cytochrome cofactor
Wolinella succinogenes
Fe2+
in the heme/cytochrome cofactor
Desulfovibrio desulfuricans
Mo(VI)
-
Anaeromyxobacter dehalogenans
Mo(VI)
-
Bradyrhizobium japonicum
Mo(VI)
-
Campylobacter jejuni subsp. jejuni
Mo(VI)
coordinates a cysteine and a sulfido residue
Cupriavidus necator
Mo(VI)
-
Desulfitobacterium hafniense
Mo(VI)
coordinates a cysteine and a sulfido residue
Escherichia coli
Mo(VI)
-
Paracoccus denitrificans
Mo(VI)
coordinates a cysteine and a sulfido residue
Paracoccus pantotrophus
Mo(VI)
coordinates a cysteine and a sulfido residue
Pseudomonas sp.
Mo(VI)
coordinates a cysteine and a sulfido residue
Rhodobacter sphaeroides
Mo(VI)
coordinates a cysteine and a sulfido residue
Shewanella gelidimarina
Mo(VI)
-
Shewanella oneidensis
Mo(VI)
-
Wolinella succinogenes
Mo(VI)
coordinates a cysteine and a sulfido residue
Desulfovibrio desulfuricans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
Wolinella succinogenes
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Shewanella oneidensis
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Desulfovibrio desulfuricans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus pantotrophus
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Pseudomonas sp.
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Cupriavidus necator
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Shewanella gelidimarina
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Desulfitobacterium hafniense
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Anaeromyxobacter dehalogenans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Campylobacter jejuni subsp. jejuni
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus denitrificans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Bradyrhizobium japonicum
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Escherichia coli
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Campylobacter jejuni subsp. jejuni ATCC 700819
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Pseudomonas sp. G-179
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus pantotrophus GB17
-
2 ferricytochrome + nitrite
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Anaeromyxobacter dehalogenans
Q2IPE7
-
-
Bradyrhizobium japonicum
A0A0M9B706
-
-
Campylobacter jejuni subsp. jejuni
Q9PPD9
-
-
Campylobacter jejuni subsp. jejuni ATCC 700819
Q9PPD9
-
-
Cupriavidus necator
P39185
-
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
P39185
-
-
Desulfitobacterium hafniense
A0A098B5Y5
-
-
Desulfovibrio desulfuricans
P81186
-
-
Escherichia coli
P33937
-
-
Paracoccus denitrificans
A1BB88
-
-
Paracoccus pantotrophus
Q56350
-
-
Paracoccus pantotrophus GB17
Q56350
-
-
Pseudomonas sp.
Q9RC05
-
-
Pseudomonas sp. G-179
Q9RC05
-
-
Rhodobacter sphaeroides
Q53176
-
-
Shewanella gelidimarina
E2F391
-
-
Shewanella oneidensis
-
-
-
Wolinella succinogenes
-
-
-
Reaction
Reaction
Commentary
Organism
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Anaeromyxobacter dehalogenans
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Bradyrhizobium japonicum
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Campylobacter jejuni subsp. jejuni
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Cupriavidus necator
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Desulfitobacterium hafniense
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Desulfovibrio desulfuricans
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Escherichia coli
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Paracoccus denitrificans
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Paracoccus pantotrophus
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Pseudomonas sp.
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Rhodobacter sphaeroides
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Shewanella gelidimarina
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Shewanella oneidensis
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
Wolinella succinogenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Wolinella succinogenes
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Shewanella oneidensis
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Desulfovibrio desulfuricans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus pantotrophus
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Pseudomonas sp.
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Cupriavidus necator
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Rhodobacter sphaeroides
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Shewanella gelidimarina
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Desulfitobacterium hafniense
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Anaeromyxobacter dehalogenans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Campylobacter jejuni subsp. jejuni
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus denitrificans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Bradyrhizobium japonicum
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Escherichia coli
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Campylobacter jejuni subsp. jejuni ATCC 700819
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Pseudomonas sp. G-179
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus pantotrophus GB17
2 ferricytochrome + nitrite
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Anaeromyxobacter dehalogenans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Bradyrhizobium japonicum
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Campylobacter jejuni subsp. jejuni
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Cupriavidus necator
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Desulfitobacterium hafniense
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Desulfovibrio desulfuricans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Escherichia coli
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Paracoccus denitrificans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Paracoccus pantotrophus
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Pseudomonas sp.
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Rhodobacter sphaeroides
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Shewanella gelidimarina
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Shewanella oneidensis
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Wolinella succinogenes
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome c
-
Anaeromyxobacter dehalogenans
cytochrome c
-
Bradyrhizobium japonicum
cytochrome c
-
Campylobacter jejuni subsp. jejuni
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Cupriavidus necator
cytochrome c
-
Desulfitobacterium hafniense
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Desulfovibrio desulfuricans
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Escherichia coli
cytochrome c
-
Paracoccus denitrificans
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Paracoccus pantotrophus
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Pseudomonas sp.
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Rhodobacter sphaeroides
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Shewanella gelidimarina
cytochrome c
-
Shewanella oneidensis
cytochrome c
-
Wolinella succinogenes
molybdenum cofactor
-
Anaeromyxobacter dehalogenans
molybdenum cofactor
-
Bradyrhizobium japonicum
molybdenum cofactor
-
Campylobacter jejuni subsp. jejuni
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Cupriavidus necator
molybdenum cofactor
-
Desulfitobacterium hafniense
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Desulfovibrio desulfuricans
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Escherichia coli
molybdenum cofactor
-
Paracoccus denitrificans
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Paracoccus pantotrophus
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Pseudomonas sp.
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Rhodobacter sphaeroides
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Shewanella gelidimarina
molybdenum cofactor
-
Shewanella oneidensis
molybdenum cofactor
-
Wolinella succinogenes
[4Fe-4S] cluster
-
Anaeromyxobacter dehalogenans
[4Fe-4S] cluster
-
Bradyrhizobium japonicum
[4Fe-4S] cluster
-
Campylobacter jejuni subsp. jejuni
[4Fe-4S] cluster
-
Cupriavidus necator
[4Fe-4S] cluster
-
Desulfitobacterium hafniense
[4Fe-4S] cluster
-
Desulfovibrio desulfuricans
[4Fe-4S] cluster
-
Paracoccus denitrificans
[4Fe-4S] cluster
-
Paracoccus pantotrophus
[4Fe-4S] cluster
-
Pseudomonas sp.
[4Fe-4S] cluster
-
Rhodobacter sphaeroides
[4Fe-4S] cluster
-
Shewanella gelidimarina
[4Fe-4S] cluster
-
Shewanella oneidensis
[4Fe-4S] cluster
-
Wolinella succinogenes
[4Fe-4S] cluster
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
gene nap and nap gene cluster, genetic organization and sequence comparisons
Anaeromyxobacter dehalogenans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Bradyrhizobium japonicum
gene nap and nap gene cluster, genetic organization and sequence comparisons
Campylobacter jejuni subsp. jejuni
gene nap and nap gene cluster, genetic organization and sequence comparisons
Cupriavidus necator
gene nap and nap gene cluster, genetic organization and sequence comparisons
Desulfitobacterium hafniense
gene nap and nap gene cluster, genetic organization and sequence comparisons
Desulfovibrio desulfuricans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Escherichia coli
gene nap and nap gene cluster, genetic organization and sequence comparisons
Paracoccus denitrificans
gene nap and nap gene cluster, genetic organization and sequence comparisons
Paracoccus pantotrophus
gene nap and nap gene cluster, genetic organization and sequence comparisons
Pseudomonas sp.
gene nap and nap gene cluster, genetic organization and sequence comparisons
Rhodobacter sphaeroides
gene nap and nap gene cluster, genetic organization and sequence comparisons
Shewanella gelidimarina
gene nap and nap gene cluster, genetic organization and sequence comparisons
Shewanella oneidensis
gene nap and nap gene cluster, genetic organization and sequence comparisons
Wolinella succinogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome c
-
Anaeromyxobacter dehalogenans
cytochrome c
-
Bradyrhizobium japonicum
cytochrome c
-
Campylobacter jejuni subsp. jejuni
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Cupriavidus necator
cytochrome c
-
Desulfitobacterium hafniense
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Desulfovibrio desulfuricans
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Escherichia coli
cytochrome c
-
Paracoccus denitrificans
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Paracoccus pantotrophus
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Pseudomonas sp.
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Rhodobacter sphaeroides
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
Shewanella gelidimarina
cytochrome c
-
Shewanella oneidensis
cytochrome c
-
Wolinella succinogenes
molybdenum cofactor
-
Anaeromyxobacter dehalogenans
molybdenum cofactor
-
Bradyrhizobium japonicum
molybdenum cofactor
-
Campylobacter jejuni subsp. jejuni
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Cupriavidus necator
molybdenum cofactor
-
Desulfitobacterium hafniense
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Desulfovibrio desulfuricans
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Escherichia coli
molybdenum cofactor
-
Paracoccus denitrificans
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Paracoccus pantotrophus
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Pseudomonas sp.
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Rhodobacter sphaeroides
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
Shewanella gelidimarina
molybdenum cofactor
-
Shewanella oneidensis
molybdenum cofactor
-
Wolinella succinogenes
[4Fe-4S] cluster
-
Anaeromyxobacter dehalogenans
[4Fe-4S] cluster
-
Bradyrhizobium japonicum
[4Fe-4S] cluster
-
Campylobacter jejuni subsp. jejuni
[4Fe-4S] cluster
-
Cupriavidus necator
[4Fe-4S] cluster
-
Desulfitobacterium hafniense
[4Fe-4S] cluster
-
Desulfovibrio desulfuricans
[4Fe-4S] cluster
-
Paracoccus denitrificans
[4Fe-4S] cluster
-
Paracoccus pantotrophus
[4Fe-4S] cluster
-
Pseudomonas sp.
[4Fe-4S] cluster
-
Rhodobacter sphaeroides
[4Fe-4S] cluster
-
Shewanella gelidimarina
[4Fe-4S] cluster
-
Shewanella oneidensis
[4Fe-4S] cluster
-
Wolinella succinogenes
[4Fe-4S] cluster
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Anaeromyxobacter dehalogenans
-
-
periplasm
-
Bradyrhizobium japonicum
-
-
periplasm
-
Campylobacter jejuni subsp. jejuni
-
-
periplasm
-
Cupriavidus necator
-
-
periplasm
-
Desulfitobacterium hafniense
-
-
periplasm
-
Escherichia coli
-
-
periplasm
-
Paracoccus denitrificans
-
-
periplasm
-
Paracoccus pantotrophus
-
-
periplasm
-
Pseudomonas sp.
-
-
periplasm
-
Rhodobacter sphaeroides
-
-
periplasm
-
Shewanella gelidimarina
-
-
periplasm
-
Shewanella oneidensis
-
-
periplasm
-
Wolinella succinogenes
-
-
periplasm
-
Desulfovibrio desulfuricans
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
in the heme/cytochrome cofactor
Anaeromyxobacter dehalogenans
Fe2+
in the heme/cytochrome cofactor
Bradyrhizobium japonicum
Fe2+
in the heme/cytochrome cofactor
Campylobacter jejuni subsp. jejuni
Fe2+
in the heme/cytochrome cofactor
Cupriavidus necator
Fe2+
in the heme/cytochrome cofactor
Desulfitobacterium hafniense
Fe2+
in the heme/cytochrome cofactor
Escherichia coli
Fe2+
in the heme/cytochrome cofactor
Paracoccus denitrificans
Fe2+
in the heme/cytochrome cofactor
Paracoccus pantotrophus
Fe2+
in the heme/cytochrome cofactor
Pseudomonas sp.
Fe2+
in the heme/cytochrome cofactor
Rhodobacter sphaeroides
Fe2+
in the heme/cytochrome cofactor
Shewanella gelidimarina
Fe2+
in the heme/cytochrome cofactor
Shewanella oneidensis
Fe2+
in the heme/cytochrome cofactor
Wolinella succinogenes
Fe2+
in the heme/cytochrome cofactor
Desulfovibrio desulfuricans
Mo(VI)
-
Anaeromyxobacter dehalogenans
Mo(VI)
-
Bradyrhizobium japonicum
Mo(VI)
-
Campylobacter jejuni subsp. jejuni
Mo(VI)
coordinates a cysteine and a sulfido residue
Cupriavidus necator
Mo(VI)
-
Desulfitobacterium hafniense
Mo(VI)
coordinates a cysteine and a sulfido residue
Escherichia coli
Mo(VI)
-
Paracoccus denitrificans
Mo(VI)
coordinates a cysteine and a sulfido residue
Paracoccus pantotrophus
Mo(VI)
coordinates a cysteine and a sulfido residue
Pseudomonas sp.
Mo(VI)
coordinates a cysteine and a sulfido residue
Rhodobacter sphaeroides
Mo(VI)
coordinates a cysteine and a sulfido residue
Shewanella gelidimarina
Mo(VI)
-
Shewanella oneidensis
Mo(VI)
-
Wolinella succinogenes
Mo(VI)
coordinates a cysteine and a sulfido residue
Desulfovibrio desulfuricans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
Wolinella succinogenes
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Shewanella oneidensis
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Desulfovibrio desulfuricans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus pantotrophus
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Pseudomonas sp.
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Cupriavidus necator
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Rhodobacter sphaeroides
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Shewanella gelidimarina
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Desulfitobacterium hafniense
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Anaeromyxobacter dehalogenans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Campylobacter jejuni subsp. jejuni
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus denitrificans
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Bradyrhizobium japonicum
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Escherichia coli
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Campylobacter jejuni subsp. jejuni ATCC 700819
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Pseudomonas sp. G-179
-
2 ferricytochrome + nitrite
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
Paracoccus pantotrophus GB17
-
2 ferricytochrome + nitrite
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Wolinella succinogenes
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Shewanella oneidensis
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Desulfovibrio desulfuricans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus pantotrophus
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Pseudomonas sp.
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Cupriavidus necator
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Rhodobacter sphaeroides
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Shewanella gelidimarina
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Desulfitobacterium hafniense
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Anaeromyxobacter dehalogenans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Campylobacter jejuni subsp. jejuni
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus denitrificans
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Bradyrhizobium japonicum
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Escherichia coli
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Campylobacter jejuni subsp. jejuni ATCC 700819
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Pseudomonas sp. G-179
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
-
742319
Paracoccus pantotrophus GB17
2 ferricytochrome + nitrite
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Anaeromyxobacter dehalogenans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Bradyrhizobium japonicum
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Campylobacter jejuni subsp. jejuni
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Cupriavidus necator
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Desulfitobacterium hafniense
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Desulfovibrio desulfuricans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Escherichia coli
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Paracoccus denitrificans
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Paracoccus pantotrophus
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Pseudomonas sp.
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Rhodobacter sphaeroides
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Shewanella gelidimarina
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Shewanella oneidensis
More
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
Wolinella succinogenes
General Information
General Information
Commentary
Organism
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Anaeromyxobacter dehalogenans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Bradyrhizobium japonicum
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Campylobacter jejuni subsp. jejuni
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Cupriavidus necator
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Desulfitobacterium hafniense
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Desulfovibrio desulfuricans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Escherichia coli
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Paracoccus denitrificans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Paracoccus pantotrophus
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Pseudomonas sp.
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Rhodobacter sphaeroides
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Shewanella gelidimarina
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Shewanella oneidensis
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Wolinella succinogenes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Cupriavidus necator
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA, product of the napA gene, is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
Desulfovibrio desulfuricans
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
Escherichia coli
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Paracoccus pantotrophus
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
Pseudomonas sp.
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Rhodobacter sphaeroides
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Shewanella gelidimarina
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Cupriavidus necator
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Paracoccus pantotrophus
physiological function
the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Rhodobacter sphaeroides
physiological function
the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Shewanella gelidimarina
General Information (protein specific)
General Information
Commentary
Organism
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Anaeromyxobacter dehalogenans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Bradyrhizobium japonicum
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Campylobacter jejuni subsp. jejuni
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Cupriavidus necator
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Desulfitobacterium hafniense
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Desulfovibrio desulfuricans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Escherichia coli
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Paracoccus denitrificans
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Paracoccus pantotrophus
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Pseudomonas sp.
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Rhodobacter sphaeroides
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
Shewanella gelidimarina
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Shewanella oneidensis
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
Wolinella succinogenes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Cupriavidus necator
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA, product of the napA gene, is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
Desulfovibrio desulfuricans
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
Escherichia coli
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Paracoccus pantotrophus
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
Pseudomonas sp.
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Rhodobacter sphaeroides
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
Shewanella gelidimarina
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Cupriavidus necator
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Paracoccus pantotrophus
physiological function
the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Rhodobacter sphaeroides
physiological function
the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
Shewanella gelidimarina
Other publictions for EC 1.9.6.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741478
Cerqueira
Periplasmic nitrate reductase ...
Desulfovibrio desulfuricans, Methylotenera mobilis, Methylotenera mobilis JLW8
Acc. Chem. Res.
48
2875-2884
2015
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742645
Lopez
The periplasmic nitrate reduc ...
Salmonella enterica, Salmonella enterica SL1344 AND CAL128
Infect. Immun.
83
3470-3478
2015
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3
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741958
Jacques
Kinetics of substrate inhibit ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides DSM 158
Biochim. Biophys. Acta
1837
1801-1809
2014
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742380
Sanchez
The nitrate-sensing NasST sys ...
Bradyrhizobium japonicum, Bradyrhizobium japonicum JCM 10833
Environ. Microbiol.
16
3263-3274
2014
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742486
Dow
Characterization of a peripla ...
Escherichia coli
FEBS J.
281
246-260
2014
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742319
Gonzalez
-
Periplasmic nitrate reductase ...
Anaeromyxobacter dehalogenans, Bradyrhizobium japonicum, Campylobacter jejuni subsp. jejuni, Campylobacter jejuni subsp. jejuni ATCC 700819, Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, Desulfitobacterium hafniense, Desulfovibrio desulfuricans, Escherichia coli, Paracoccus denitrificans, Paracoccus pantotrophus, Paracoccus pantotrophus GB17, Pseudomonas sp., Pseudomonas sp. G-179, Rhodobacter sphaeroides, Shewanella gelidimarina, Shewanella oneidensis, Wolinella succinogenes
Coord. Chem. Rev.
257
315-331
2013
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28
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742648
Cerqueira
The sulfur shift an activatio ...
Desulfovibrio desulfuricans
Inorg. Chem.
52
10766-10772
2013
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712967
Simpson
The periplasmic nitrate reduct ...
Shewanella amazonensis, Shewanella amazonensis SB2B, Shewanella baltica, Shewanella baltica OS155, Shewanella baltica OS185, Shewanella baltica OS195, Shewanella baltica OS223, Shewanella denitrificans, Shewanella denitrificans OS217, Shewanella frigidimarina, Shewanella halifaxensis, Shewanella loihica, Shewanella loihica PV-4, Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550, Shewanella pealeana, Shewanella piezotolerans, Shewanella piezotolerans WP3, Shewanella putrefaciens, Shewanella putrefaciens CN-32, Shewanella sediminis, Shewanella sp., Shewanella sp. ANA-3, Shewanella sp. MR-4, Shewanella sp. MR-7, Shewanella sp. W3-18-1, Shewanella woodyi
Microbiology
156
302-312
2010
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696917
Durvasula
Effect of periplasmic nitrate ...
Paracoccus pantotrophus
Biotechnol. Prog.
25
973-979
2009
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698636
Stewart
Catabolite repression control ...
Paracoccus pantotrophus
J. Bacteriol.
191
996-1005
2009
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699015
Hofmann
Density functional theory stud ...
Desulfovibrio desulfuricans
J. Biol. Inorg. Chem.
14
1023-1035
2009
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699199
Cerqueira
The effect of the sixth sulfur ...
Desulfovibrio desulfuricans
J. Comput. Chem.
30
2466-2484
2009
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711653
Van Alst
Compensatory periplasmic nitra ...
Pseudomonas aeruginosa
Can. J. Microbiol.
55
1133-1144
2009
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684990
Gates
Voltammetric characterization ...
Paracoccus pantotrophus
Biochem. J.
409
159-168
2008
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695337
Coelho
Heterodimeric nitrate reductas ...
Cupriavidus necator H16
Acta Crystallogr. Sect. F
63
516-519
2007
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674891
Jepson
Spectropotentiometric and stru ...
Escherichia coli
J. Biol. Chem.
282
6425-6437
2006
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675847
Nilavongse
The NapF protein of the Escher ...
Escherichia coli
Microbiology
152
3227-3237
2006
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