Information on EC 1.7.99.4 - nitrate reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
1.7.99.4
-
RECOMMENDED NAME
GeneOntology No.
nitrate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nitrite + acceptor = nitrate + reduced acceptor
show the reaction diagram
mechanism of respiratory-driven proton translocation
-
nitrite + acceptor = nitrate + reduced acceptor
show the reaction diagram
mechanism of respiratory-driven proton translocation
Escherichia coli EMG-2
-
-
nitrite + acceptor = nitrate + reduced acceptor
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Halomonas sp.
-
-
oxidation
Halomonas sp. AGJ1-3
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
-
reduction
Halomonas sp.
-
-
reduction
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
-
reduction
-
-
reduction
Halomonas sp. AGJ1-3
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
-
nitrate reduction I (denitrification)
-
nitrate reduction VII (denitrification)
-
Nitrogen metabolism
-
SYSTEMATIC NAME
IUBMB Comments
nitrite:acceptor oxidoreductase
The Pseudomonas enzyme is a cytochrome, but the enzyme from Micrococcus halodenitrificans is an iron protein containing molybdenum. Reduced benzyl viologen and other dyes bring about the reduction of nitrate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
assimilatory nitrate reductases
-
Nas enzyme
Cytochrome B-NR
-
-
-
-
dissimilatory nitrate reductase
-
-
NAP
-
periplasmic respiratory nitrate reductase
NAP
-
periplasmic respiratory nitrate reductase
-
NAP
-
periplasmic respiratory nitrate reductase
NapA
Salmonella enterica subsp. enterica serovar Typhimurium SL1344
E1WCA0
-
-
NapA
Q7M962
in order to catalyse nitrate reduction Epsilonproteobacteria encode the periplasmic nitrate reductase system (Nap) whereas genes encoding the subunits of the membrane-bound nitrate reductase complex (NarGHI) are absent
NaR
-
-
-
-
NaR
Gordonia alkanivorans S7
-
-
-
NarC/NarI/NarG/NarH
-
-
nitrate reductase
-
-
nitrate reductase
-
-
nitrate reductase
Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
-
nitrate reductase
Halomonas sp.
-
-
nitrate reductase
Halomonas sp. AGJ1-3
-
-
-
nitrate reductase
-
-
nitrate reductase
-
-
nitrate reductase
-
-
nitrate reductase (acceptor)
-
-
-
-
periplasmic nitrate reductase
-
Nap enzyme
reductase, nitrate (acceptor)
-
-
-
-
respiratory nitrate reductase
-
-
-
-
respiratory nitrate reductase
-
Nar enzyme
respiratory nitrate reductase
P85098 and P85097
-
respiratory nitrate reductase
Bradyrhizobium sp. USDA 3045
P85098 and P85097
-
-
respiratory nitrate reductase
-
-
respiratory nitrate reductase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37256-45-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cultivar Smooth Cayenne
UniProt
Manually annotated by BRENDA team
cultivar Col-1
-
-
Manually annotated by BRENDA team
strain Sp245, NAP is expressed under oxic and anoxic conditions
-
-
Manually annotated by BRENDA team
strain Sp245, NAP is expressed under oxic and anoxic conditions
-
-
Manually annotated by BRENDA team
Bacillus licheniformis S244
strain S244
-
-
Manually annotated by BRENDA team
inoculated to root nodules of Glycine max. In the presence of nitrate, all of the nitrosylleg-hemoglobin within normoxic nodules arises from nitrate reduction by the bacterial enzyme, whereas the enzyme is only responsible for half of the nitrosylleg-hemoglobin within hypoxic nodules
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum USDA110
USDA110
-
-
Manually annotated by BRENDA team
P85098: respiratory nitrate reductase beta chain, P85097: respiratory nitrate reductase alpha chain; strain USDA 3045
P85098 and P85097
UniProt
Manually annotated by BRENDA team
strain USDA 3045
-
-
Manually annotated by BRENDA team
Bradyrhizobium sp. USDA 3045
P85098: respiratory nitrate reductase beta chain, P85097: respiratory nitrate reductase alpha chain; strain USDA 3045
P85098 and P85097
UniProt
Manually annotated by BRENDA team
Bradyrhizobium sp. USDA 3045
strain USDA 3045
-
-
Manually annotated by BRENDA team
strain ATCC 27774
-
-
Manually annotated by BRENDA team
2 forms: nitrate reductase I: ab, nitrate reductase II: abc2 and (abc2)4
-
-
Manually annotated by BRENDA team
2 forms: nitrate reductase I: ab, nitrate reductase II: abc2 and (abc2)4; identical with Aerobacter aerogenes; strain S 45
-
-
Manually annotated by BRENDA team
strain IFO 12935
-
-
Manually annotated by BRENDA team
Enterobacter cloacae IFO 12935
strain IFO 12935
-
-
Manually annotated by BRENDA team
2 forms of enzyme: monomeric and probably tetrameric form; strain A1002; strain K12
-
-
Manually annotated by BRENDA team
coexistence of 2 enzyme forms with different subunit compositions; strain K12
-
-
Manually annotated by BRENDA team
respiratory nitrate reductase 1 alpha chain
UniProt
Manually annotated by BRENDA team
strain A1004a, 5-aminolaevulinic acid auxotroph
-
-
Manually annotated by BRENDA team
strain EMG 29
-
-
Manually annotated by BRENDA team
strain EMG-2
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain K12; strain RK7
-
-
Manually annotated by BRENDA team
strain K12; strain X5119
-
-
Manually annotated by BRENDA team
Escherichia coli A1002
strain A1002
-
-
Manually annotated by BRENDA team
Escherichia coli A1004a
strain A1004a, 5-aminolaevulinic acid auxotroph
-
-
Manually annotated by BRENDA team
Escherichia coli EMG
strain EMG 29
-
-
Manually annotated by BRENDA team
Escherichia coli EMG-2
strain EMG-2
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli RK7
strain RK7
-
-
Manually annotated by BRENDA team
Escherichia coli X5119
strain X5119
-
-
Manually annotated by BRENDA team
Fusarium oxysporum 11dn1
-
-
Manually annotated by BRENDA team
NCA strain 2184, identical with ATCC 12016
-
-
Manually annotated by BRENDA team
Gordonia alkanivorans S7
-
-
-
Manually annotated by BRENDA team
extreme halophile
-
-
Manually annotated by BRENDA team
halophilic archaeon
-
-
Manually annotated by BRENDA team
induction of enzyme activity under anaerobic conditions using nitrate as a terminal electron acceptor. Strain grows in the presence of nitrite concentrations as high as 40 mM
-
-
Manually annotated by BRENDA team
halophilic archaeon
-
-
Manually annotated by BRENDA team
strain ATCC 13511, moderate halophile, nitrate reductase A
-
-
Manually annotated by BRENDA team
NarG
SwissProt
Manually annotated by BRENDA team
NarH
SwissProt
Manually annotated by BRENDA team
NarI
SwissProt
Manually annotated by BRENDA team
NarJ
SwissProt
Manually annotated by BRENDA team
NarK
SwissProt
Manually annotated by BRENDA team
Halomonas sp.
strain AGJ1-3
-
-
Manually annotated by BRENDA team
Halomonas sp. AGJ1-3
strain AGJ1-3
-
-
Manually annotated by BRENDA team
Marinobacter hydrocarbonoclasticus 617
strain 617
-
-
Manually annotated by BRENDA team
formerly Micrococcus denitrificans
-
-
Manually annotated by BRENDA team
strain NCIB 8944
-
-
Manually annotated by BRENDA team
Paracoccus denitrificans NCIB 8944
strain NCIB 8944
-
-
Manually annotated by BRENDA team
enzymic activty only after growth on molybdate or tungstate
-
-
Manually annotated by BRENDA team
strain LMD82.5, expression of two catalytically distinct forms: a membrane-bound form under anaerobic growth conditions and a periplasmic form mainly under aerobic growth conditions
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus LMD82.5
strain LMD82.5, expression of two catalytically distinct forms: a membrane-bound form under anaerobic growth conditions and a periplasmic form mainly under aerobic growth conditions
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus M-6
strain M-6
-
-
Manually annotated by BRENDA team
strain ATCC 13867
-
-
Manually annotated by BRENDA team
only membrane-bound nitrate reductase A, no periplasmic enzyme; strain YT101
-
-
Manually annotated by BRENDA team
strain YT101
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens YT101
strain YT101
-
-
Manually annotated by BRENDA team
formerly Pseudomonas perfectomarina; strain ATCC 14405
-
-
Manually annotated by BRENDA team
strain ATCC 14405
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
f. sp. denitrificans IL106
-
-
Manually annotated by BRENDA team
f.sp. denitrificans, strain IL106
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides f. sp. denitrificans
-
-
Manually annotated by BRENDA team
strain DSM158, in vitro enzyme activity after different growth conditions
-
-
Manually annotated by BRENDA team
Rhodobacter sphaeroides DSM158
strain DSM158, in vitro enzyme activity after different growth conditions
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium SL1344
-
E1WCA0
UniProt
Manually annotated by BRENDA team
strain RF-1, diazotrophically growing cells
-
-
Manually annotated by BRENDA team
Synechococcus sp. RF-1
strain RF-1, diazotrophically growing cells
-
-
Manually annotated by BRENDA team
strain HB8, ATCC 27643
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
nitrate reductase activity is needed to nitric oxide synthesis in roots
physiological function
E1WCA0
under nitrate-rich conditions, the nar and nap genes encoding a membrane-bound form and a periplasmic form of nitrate reductase, as well as NO-regulated genes encoding flavohaemoglobin, flavorubredoxin and hybrid cluster protein are induced following transition from the oxic to anoxic state, and 20% of nitrate consumed in steady-state is released as N2O when nitrite has accumulated to millimolar levels. The kinetics of nitrate consumption, nitrite accumulation and N2O production are similar to those of wild-type in nitrate-sufficient cultures of a nap mutant. Under nitrate-limited conditions, periplasmic enzyme nap, but not nar, is upregulated following transition from oxic to anoxic metabolism and very little N2O production was observedA combination of nitrate-sufficiency, nitrite accumulation and an active Nar-type nitrate reductase leads to NO and thence N2O production, and this can account for up to 20% of the nitrate catabolized
physiological function
A4U4X7, -
deletion of nap gene abolishes anaerobic growth and also delays aerobic growth in both nitrate and ammonium media. Deletion of nap gene severely impairs magnetite biomineralization and results in fewer, smaller, and irregular crystals during denitrification and also microaerobic respiration, probably by disturbing the proper redox balance required for magnetite synthesis. In contrast to the case for the wild type, biomineralization in nap deletion cells is independent of the oxidation state of carbon substrate
physiological function
Salmonella enterica subsp. enterica serovar Typhimurium SL1344
-
under nitrate-rich conditions, the nar and nap genes encoding a membrane-bound form and a periplasmic form of nitrate reductase, as well as NO-regulated genes encoding flavohaemoglobin, flavorubredoxin and hybrid cluster protein are induced following transition from the oxic to anoxic state, and 20% of nitrate consumed in steady-state is released as N2O when nitrite has accumulated to millimolar levels. The kinetics of nitrate consumption, nitrite accumulation and N2O production are similar to those of wild-type in nitrate-sufficient cultures of a nap mutant. Under nitrate-limited conditions, periplasmic enzyme nap, but not nar, is upregulated following transition from oxic to anoxic metabolism and very little N2O production was observedA combination of nitrate-sufficiency, nitrite accumulation and an active Nar-type nitrate reductase leads to NO and thence N2O production, and this can account for up to 20% of the nitrate catabolized
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
-
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
-
-
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
-
-
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
membrane-bound enzyme form uses chlorate as substrate, but not periplasmic form
-
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
substrate for purified enzyme, but no substrate in intact cells
-
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
slightly higher rate than with nitrate, but weaker enzyme affinity for chlorate than for nitrate
-
?
chlorate + reduced acceptor
chlorite + acceptor
show the reaction diagram
-
alternative electron acceptor to nitrate
-
-
?
chlorate + reduced acceptor
?
show the reaction diagram
Halomonas sp., Halomonas sp. AGJ1-3
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced cytochrome b as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
electron donor and acceptor have different binding sites
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
NADH as electron donor, only membrane-bound enzyme form
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
cytochrome-containing enzyme uses duroquinol as electron donor, but not cytochrome-free enzyme, reduction rate is 50 times slower compared with reduced methyl viologen as electron donor, ascorbate-phenazine methosulfate as electron donor for cytochrome-containing enzyme, reduced viologen indicators as electron donors
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced viologen indicators as electron donors
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced viologen indicators as electron donors
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced viologen indicators as electron donors
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
enzyme reacts with FMNH2 at the inner aspect of the cytoplasmic membrane and can catalyze a vectorial reduction of nitrate on the outer aspect with reducing equivalents from the inner aspect
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen with 109% and FADH2 with 8% of the rate obtained with reduced methyl viologen, catalyzes terminal reaction of a proton-translocating respiratory chain with a two electron transfer from nitrate to nitrite
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
in vitro artificial electron donors, e.g. reduced viologen indicators, can replace cytochrome c, reduction of cytochrome b556 by ubiquinol which releases two protons, electrons are passed to nitrate reductase and used to reduce NO3- to NO2-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
transfer of reducing equivalents from reduced ubiquinol via cytochrome b-556 and nitrate reductase to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
cytochrome c-552 may be an electron donor for enzyme
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
genetic and/or functional relationship between the dissimilatory reduction of nitrate and that of nitrite
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
presence of a functional structural gene encoding the respiratory nitrate reductase confers higher rhizosphere competence of maize
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
physiological rate of nitrate reduction by the respiratory chain is saturated by 0.04 mM nitrate or less, lower rate compared to the rate obtained with reduced benzyl viologen, enzyme may act as a transmembrane hydrogen carrier
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
NarC, a 27 kDa membrane cytochrome c, plays an essential role in the synthesis of active enzyme and for the attachment of enzyme to the membrane, role of NarC as a component of the electron transport chain toward the NR
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
gamma-subunit catalyzes electron transfer to the alpha- and beta-subunits from physiologically ubiquinol which acts as branch point in the respiratory chain, electron flow from ubiquinol via cytochrome b on the periplasmic side of membrane to enzyme active site at the cytoplasmic side
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
first step of an aerobic denitrification process in presence of oxygen
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
linked to the respiratory chain at the level of the quinol pool in the cytoplasmic membrane
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
physiological function: transfer of electrons from cytochrome b559 to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
bacterial denitrification
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
the enzyme is responsible for anaerobic growth of Bradyrhizobium japonicum under nitrate-respiring conditions
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration catalysed by the epsilon-proteobacterium Wolinella succinogenes relies on the NapAGHBFLD system that comprises periplasmic nitrate reductase (NapA) and various other Nap proteins required for electron transport from menaquinol to NapA or maturation of Nap components. In the Wolinella succinogenes Nap system electron transfer to NapA depends on both subunits of the predicted menaquinol dehydrogenase complex NapGH but does not require a cytochrome c of the NapC/NrfH family. The iron-sulfur protein NapG forms a complex with NapH in the membrane but is detected in the periplasmic cell fraction in the absence of NapH. NapG is a specific adapter proteins that channels electrons into either the Nap or Nos system
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Q7M962
the membrane-bound formate dehydrogenase (FdhABC) and Ni/Fe-hydrogenase (HydABC) complexes of Wolinella succinogenes couple the oxidation of formate or hydrogen to the reduction of membraneous menaquinone-6 thereby generating an electrochemical proton gradient according to the redox loop mechanism. Therefore, in principal, the participation of such an enzyme complex is sufficient to sustain growth irrespective of whether or not the menaquinone-replenishing oxidation of menaquinol by an appropriate electron acceptor is catalysed in an electrogenic fashion. In fact, each of the menaquinol-oxidizing systems that transfer electrons to the terminal reductases NapA (nitrate reductase), NrfA (nitrite ammonification) and cNosZ (nitrous oxide reduction to dinitrogen) appear to catalyse electroneutral reactions, the membrane-bound formate dehydrogenase (FdhABC) and Ni/Fe-hydrogenase (HydABC) complexes of Wolinella succinogenes couple the oxidation of formate or hydrogen to the reduction of membraneous menaquinone-6 thereby generating an electrochemical proton gradient according to the redox loop mechanism. Therefore, in principal, the participation of such an enzyme complex is sufficient to sustain growth irrespective of whether or not the menaquinone-replenishing oxidation of menaquinol by an appropriate electron acceptor is catalysed in an electrogenic fashion. In fact, each of the menaquinol-oxidizing systems that transfer electrons to the terminal reductases NapA (nitrate reductase), NrfA (reduction of nitrite to ammonia) and cNosZ (nitrous oxide reduction to dinitrogen) appear to catalyse electroneutral reactions. Nitrate is reduced by a periplasmic NapAB complex that is likely to be reduced by the membrane-bound menaquinol dehydrogenase complex NapGH. The molybdenum cofactor (Mo) and the ironsulfur centre of NapA are attached in the cytoplasm by specific maturation systems prior to Holo-NapA export by the twin-arginine translocation (Tat) complex. The chaperone NapD is required to coordinate maturation and export of NapA
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
Wolinella succinogenes transfers electrons from formate via the menaquinone pool to NapA independently of a membrane-bound c-type cytochrome of the NapC family
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus denitrificans NCIB 8944
-
reduced methyl viologen as electron donor, cytochrome-containing enzyme uses duroquinol as electron donor, but not cytochrome-free enzyme, reduction rate is 50 times slower compared with reduced methyl viologen as electron donor, ascorbate-phenazine methosulfate as electron donor for cytochrome-containing enzyme, reduced viologen indicators as electron donors
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus denitrificans NCIB 8944
-
nitrate respiration, gamma-subunit catalyzes electron transfer to the alpha- and beta-subunits from physiologically ubiquinol which acts as branch point in the respiratory chain, electron flow from ubiquinol via cytochrome b on the periplasmic side of membrane to enzyme active site at the cytoplasmic side
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG-2
-
reduced benzyl viologen as electron donor, FMNH2 as electron donor, enzyme reacts with FMNH2 at the inner aspect of the cytoplasmic membrane and can catalyze a vectorial reduction of nitrate on the outer aspect with reducing equivalents from the inner aspect
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG-2
-
physiological rate of nitrate reduction by the respiratory chain is saturated by 0.04 mM nitrate or less, lower rate compared to the rate obtained with reduced benzyl viologen, enzyme may act as a transmembrane hydrogen carrier
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
reduced benzyl viologen as electron donor, reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
linked to the respiratory chain at the level of the quinol pool in the cytoplasmic membrane
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bacillus licheniformis S244
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bacillus licheniformis S244
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bacillus licheniformis S244
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bacillus licheniformis S244
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli RK7
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
the enzyme is responsible for anaerobic growth of Bradyrhizobium japonicum under nitrate-respiring conditions
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Enterobacter cloacae IFO 12935
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Enterobacter cloacae IFO 12935
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus pantotrophus M-6
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG
-
transfer of reducing equivalents from reduced ubiquinol via cytochrome b-556 and nitrate reductase to nitrate, nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1004a
-
reduced benzyl viologen as electron donor, FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1004a
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
reduced benzyl viologen as electron donor, reduced viologen indicators as electron donors
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
reduced benzyl viologen as electron donor, FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate, nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
reduced methyl viologen as electron donor, reduced benzyl viologen with 109% and FADH2 with 8% of the rate obtained with reduced methyl viologen, catalyzes terminal reaction of a proton-translocating respiratory chain with a two electron transfer from nitrate to nitrite
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus pantotrophus LMD82.5
-
reduced benzyl viologen as electron donor, reduced methyl viologen as electron donor, NADH as electron donor, only membrane-bound enzyme form
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus pantotrophus LMD82.5
-
nitrate respiration, first step of an aerobic denitrification process in presence of oxygen
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli X5119
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli X5119
-
nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
-
-
-
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
presence of a functional structural gene encoding the respiratory nitrate reductase confers higher rhizosphere competence of maize
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
genetic and/or functional relationship between the dissimilatory reduction of nitrate and that of nitrite
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1002
-
reduced benzyl viologen as electron donor, FMNH2 as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1002
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate, nitrate respiration
-
-
?
nitrate + reduced acceptor
?
show the reaction diagram
Halomonas sp., Halomonas sp. AGJ1-3
-
-
-
-
?
nitrate + reduced acceptor
nitrite + oxidized acceptor
show the reaction diagram
P85098 and P85097
-
-
-
?
nitrate + reduced acceptor
nitrite + oxidized acceptor
show the reaction diagram
C3U5B4
-
-
-
?
nitrate + reduced acceptor
nitrite + oxidized acceptor
show the reaction diagram
-
a model of the electron transport chain of nitrate respiration is proposed in which one or more of the napF, G, H and L gene products mediate electron transport from menaquinol to the periplasmic NapAB complex
-
-
?
nitrate + reduced acceptor
nitrite + oxidized acceptor
show the reaction diagram
Bradyrhizobium sp. USDA 3045
P85098 and P85097
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor + H2O
show the reaction diagram
-
Wolinella succinogenes transfers electrons from formate via the menaquinone pool to NapA independently of a membrane-bound c-type cytochrome of the NapC family. The napB and napD gene products are essential for nitrate respiration. NapD is required for the production of mature NapA. NapF or NapL function in NapA assembly and/or export
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
show the reaction diagram
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
show the reaction diagram
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + benzyl viologen
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
show the reaction diagram
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
show the reaction diagram
Bradyrhizobium sp., Bradyrhizobium sp. USDA 3045
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
-
reduced methyl viologen is the best electron donor. NADPH or NADH show only 2.4% of maximal activity, no activity with FADH2
-
-
?
nitrate + reduced methyl viologen
nitrite + methyl viologen
show the reaction diagram
Marinobacter hydrocarbonoclasticus 617
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
show the reaction diagram
-
the purified enzyme does not react with duroquinol or NADH. It may be that the purified enzyme has lost some of the components that mediate the electron transport from the physiological reductant to the catalytic 63000 Da polypeptide during the purification process
-
-
?
nitrate + reduced methylviologen
nitrite + oxidized methyl viologen + H2O
show the reaction diagram
-
-
-
-
?
nitrate + reduced methylviologen
nitrite + oxidized methyl viologen + H2O
show the reaction diagram
-
-
-
-
?
nitrate + reduced methylviologen
nitrite + oxidized methyl viologen + H2O
show the reaction diagram
-
benzyl viologen, NADH, and reduced FAD are also readily oxidized by the complex in the presence of nitrate, suggesting that they, too, could serve as electron donors
-
-
?
nitrite + acceptor
nitrate + reduced acceptor
show the reaction diagram
-
-
-
-
-
nitrite + acceptor
nitrate + reduced acceptor
show the reaction diagram
-
-
-
-
?
reduced methyl viologen + chlorate
methyl viologen + chlorite
show the reaction diagram
Gordonia alkanivorans, Gordonia alkanivorans S7
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-
-
-
-
-
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-
-
-
-
-
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-, Q93HX3
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
-, Q93HX3
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
Synechococcus sp. RF-1
-
-
-
-
?
reduced methyl viologen + nitrate
methyl viologen + nitrite
show the reaction diagram
Gordonia alkanivorans S7
-
-
-
-
?
dithionite + methyl viologen
?
show the reaction diagram
Halomonas sp., Halomonas sp. AGJ1-3
-
activity assay
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no enzyme activity in cell extracts when methyl viologen is used as electron donor instead of benzyl viologen
-
-
-
additional information
?
-
-
not as electron donors: NADH, NADPH
-
-
-
additional information
?
-
-
not as electron donors: NADH, NADPH
-
-
-
additional information
?
-
-
not as electron donors: 2,6-dichlorophenolindophenol and horse heart cytochrome c
-
-
-
additional information
?
-
-
after solubilization and purification enzyme is no longer active with the natural electron donors NADH and formate
-
-
-
additional information
?
-
-
not as electron donor: FADH2, FMNH2, menadione
-
-
-
additional information
?
-
-
structure is folded in 4 domains with an alpha/beta-type topology, all are involved in cofactor binding
-
-
-
additional information
?
-
-
in vitro artificial electron donors, e.g. reduced viologen indicators, can replace cytochrome c
-
-
-
additional information
?
-
-
FMNH2 is a non-physiological reductant
-
-
-
additional information
?
-
-
involved in cellular redox balancing
-
-
-
additional information
?
-
-
nitrate reduction is mainly regulated at the level of enzyme activity by both nitrate and electron supply, enzyme is involved in redox balancing
-
-
-
additional information
?
-
-
the enzyme is responsible for the first step in the denitrification process
-
-
-
additional information
?
-
-
the regulation of the nar gene occurs at transcriptional level induced by oxygen-limiting conditions and the presence of nitrate
-
-
-
additional information
?
-
-
despite the capacity of Nap to reduce tellurite and selenate in vitro, the catalytic activity of the enzyme for these substrates is low and the resistance of Rhodobacter sphaeroides to these substrates cannot be attributed to their reduction by Nap
-
-
-
additional information
?
-
-
nitrate/nitrite reductase complex also catalyzes reduction of nitrite
-
-
-
additional information
?
-
-
The purified enzyme supports the catalysis of chlorate (structure homologous to nitrate). The purified enzyme does not react with duroquinol or NADH. It may be that the purified enzyme has lost some of the components that mediate the electron transport from the physiological reductant to the catalytic 63000 Da polypeptide during the purification process
-
-
-
additional information
?
-
-
enzyme is localized exclusively in spores and no exogenous electron donor is required to drive nitrate reduction
-
-
-
additional information
?
-
Escherichia coli EMG-2
-
FMNH2 is a non-physiological reductant
-
-
-
additional information
?
-
Escherichia coli K12
-
-
-
-
-
additional information
?
-
Escherichia coli K12
-
not as electron donors: 2,6-dichlorophenolindophenol and horse heart cytochrome c
-
-
-
additional information
?
-
Rhodobacter sphaeroides DSM158
-
nitrate reduction is mainly regulated at the level of enzyme activity by both nitrate and electron supply, enzyme is involved in redox balancing
-
-
-
additional information
?
-
Pseudomonas fluorescens YT101
-
no enzyme activity in cell extracts when methyl viologen is used as electron donor instead of benzyl viologen
-
-
-
additional information
?
-
Escherichia coli A1002
-
-
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
catalyzes terminal reaction of a proton-translocating respiratory chain with a two electron transfer from nitrate to nitrite
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
in vitro artificial electron donors, e.g. reduced viologen indicators, can replace cytochrome c, reduction of cytochrome b556 by ubiquinol which releases two protons, electrons are passed to nitrate reductase and used to reduce NO3- to NO2-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
transfer of reducing equivalents from reduced ubiquinol via cytochrome b-556 and nitrate reductase to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
cytochrome c-552 may be an electron donor for enzyme
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
genetic and/or functional relationship between the dissimilatory reduction of nitrate and that of nitrite
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
presence of a functional structural gene encoding the respiratory nitrate reductase confers higher rhizosphere competence of maize
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
physiological rate of nitrate reduction by the respiratory chain is saturated by 0.04 mM nitrate or less, lower rate compared to the rate obtained with reduced benzyl viologen, enzyme may act as a transmembrane hydrogen carrier
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
NarC, a 27 kDa membrane cytochrome c, plays an essential role in the synthesis of active enzyme and for the attachment of enzyme to the membrane, role of NarC as a component of the electron transport chain toward the NR
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
gamma-subunit catalyzes electron transfer to the alpha- and beta-subunits from physiologically ubiquinol which acts as branch point in the respiratory chain, electron flow from ubiquinol via cytochrome b on the periplasmic side of membrane to enzyme active site at the cytoplasmic side
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
first step of an aerobic denitrification process in presence of oxygen
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
linked to the respiratory chain at the level of the quinol pool in the cytoplasmic membrane
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
physiological function: transfer of electrons from cytochrome b559 to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
bacterial denitrification
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
the enzyme is responsible for anaerobic growth of Bradyrhizobium japonicum under nitrate-respiring conditions
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
nitrate respiration catalysed by the epsilon-proteobacterium Wolinella succinogenes relies on the NapAGHBFLD system that comprises periplasmic nitrate reductase (NapA) and various other Nap proteins required for electron transport from menaquinol to NapA or maturation of Nap components. In the Wolinella succinogenes Nap system electron transfer to NapA depends on both subunits of the predicted menaquinol dehydrogenase complex NapGH but does not require a cytochrome c of the NapC/NrfH family. The iron-sulfur protein NapG forms a complex with NapH in the membrane but is detected in the periplasmic cell fraction in the absence of NapH. NapG is a specific adapter proteins that channels electrons into either the Nap or Nos system
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Q7M962
the membrane-bound formate dehydrogenase (FdhABC) and Ni/Fe-hydrogenase (HydABC) complexes of Wolinella succinogenes couple the oxidation of formate or hydrogen to the reduction of membraneous menaquinone-6 thereby generating an electrochemical proton gradient according to the redox loop mechanism. Therefore, in principal, the participation of such an enzyme complex is sufficient to sustain growth irrespective of whether or not the menaquinone-replenishing oxidation of menaquinol by an appropriate electron acceptor is catalysed in an electrogenic fashion. In fact, each of the menaquinol-oxidizing systems that transfer electrons to the terminal reductases NapA (nitrate reductase), NrfA (nitrite ammonification) and cNosZ (nitrous oxide reduction to dinitrogen) appear to catalyse electroneutral reactions
-
-
?
nitrate + reduced acceptor
nitrite + oxidized acceptor
show the reaction diagram
-
a model of the electron transport chain of nitrate respiration is proposed in which one or more of the napF, G, H and L gene products mediate electron transport from menaquinol to the periplasmic NapAB complex
-
-
?
nitrate + reduced acceptor
nitrite + acceptor + H2O
show the reaction diagram
-
Wolinella succinogenes transfers electrons from formate via the menaquinone pool to NapA independently of a membrane-bound c-type cytochrome of the NapC family. The napB and napD gene products are essential for nitrate respiration. NapD is required for the production of mature NapA. NapF or NapL function in NapA assembly and/or export
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus denitrificans NCIB 8944
-
nitrate respiration, gamma-subunit catalyzes electron transfer to the alpha- and beta-subunits from physiologically ubiquinol which acts as branch point in the respiratory chain, electron flow from ubiquinol via cytochrome b on the periplasmic side of membrane to enzyme active site at the cytoplasmic side
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG-2
-
physiological rate of nitrate reduction by the respiratory chain is saturated by 0.04 mM nitrate or less, lower rate compared to the rate obtained with reduced benzyl viologen, enzyme may act as a transmembrane hydrogen carrier
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
-
linked to the respiratory chain at the level of the quinol pool in the cytoplasmic membrane
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bacillus licheniformis S244
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
the enzyme is responsible for anaerobic growth of Bradyrhizobium japonicum under nitrate-respiring conditions
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Enterobacter cloacae IFO 12935
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli EMG
-
transfer of reducing equivalents from reduced ubiquinol via cytochrome b-556 and nitrate reductase to nitrate, nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1004a
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate, nitrate respiration
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli K12
-
catalyzes terminal reaction of a proton-translocating respiratory chain with a two electron transfer from nitrate to nitrite
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Paracoccus pantotrophus LMD82.5
-
nitrate respiration, first step of an aerobic denitrification process in presence of oxygen
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli X5119
-
nitrate respiration, functions as a terminal enzyme of the respiratory chain, when organism is grown anaerobically in presence of nitrate as electron acceptor
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
presence of a functional structural gene encoding the respiratory nitrate reductase confers higher rhizosphere competence of maize
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Pseudomonas fluorescens YT101
-
genetic and/or functional relationship between the dissimilatory reduction of nitrate and that of nitrite
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
show the reaction diagram
Escherichia coli A1002
-
terminal oxidoreduction enzyme of a proton-translocating respiratory chain, two-electron transfer probably from a b-type cytochrome to nitrate, nitrate respiration
-
-
?
nitrite + acceptor
nitrate + reduced acceptor
show the reaction diagram
-
-
-
-
-
nitrite + acceptor
nitrate + reduced acceptor
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
FMNH2 is a non-physiological reductant
-
-
-
additional information
?
-
-
involved in cellular redox balancing
-
-
-
additional information
?
-
-
nitrate reduction is mainly regulated at the level of enzyme activity by both nitrate and electron supply, enzyme is involved in redox balancing
-
-
-
additional information
?
-
-
the enzyme is responsible for the first step in the denitrification process
-
-
-
additional information
?
-
-
the regulation of the nar gene occurs at transcriptional level induced by oxygen-limiting conditions and the presence of nitrate
-
-
-
additional information
?
-
Escherichia coli EMG-2
-
FMNH2 is a non-physiological reductant
-
-
-
additional information
?
-
Rhodobacter sphaeroides DSM158
-
nitrate reduction is mainly regulated at the level of enzyme activity by both nitrate and electron supply, enzyme is involved in redox balancing
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bactopterin
-
common cofactor of eubacterial molybdoenzymes
cytochrome b
-
in some preparations a gamma-subunit is found that is a b-type cytochrome
-
cytochrome b
-
enzyme contains a b-type cytochrome that is reduced by duroquinol and oxidized by nitrate, lack of the gamma-subunit is correlated with the lack of cytochrome b, gamma-subunit is a b-type cytochrome
-
cytochrome b
-
-
-
cytochrome b
-
0.49 mol cytochrome b per mol enzyme complex as cofactor, presence of a chlorate-oxidizable cytochrome b
-
FAD
-
assimilatory nitrate reductases
heme
-
the diheme cytochrome NsapB constitutes the small subunit of the nitrate reductase. The two heme groups have nearly parallel heme planes. van der Waals distances with an iron-to-iron distance of 9.9 A. The two propionate side chaind on both heme groups are hydrogen-bonded to each other. The propionates of one of the heme groups are pulled towards the interior of the molecule due to a salt bridge and a number of hydrogen bonds between the propionates and conserved residues
heme
-
the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA
heme b
-
an additional 20 kDa subunit is present in heme-containing enzyme
heme b
-
NarI subunit of the respiratory nitrate reductases
heme b
-
contains one heme per enzyme molecule
Heme c
-
the 62000 Da polypeptide (a low-midpoint potential (207 mV), multiheme cytochrome c) exhibits nitrite reductase activity under denaturing conditions
Heme c
-
contains 0.4 heme c per enzyme molecule
iron-sulfur centre
-
enzyme contains iron-sulfur centres
iron-sulfur centre
-
enzyme contains 2 non-heme Fe atoms and 4 labile sulfide groups in acid medium per enzyme molecule
iron-sulfur centre
-
molybdo-iron-sulfur protein
iron-sulfur centre
-
molybdo-iron-sulfur protein; nitrate reductase I, MW 260000, abc2: 8 iron-sulfur groups per molecule of enzyme, which participate in electron transfer
iron-sulfur centre
-
6 atoms of non-heme iron and 12 mol of labile sulfide in 1 mol of purified enzyme
iron-sulfur centre
-
16 g atoms of iron and 14 g atoms of acid-labile sulfide per mol of enzyme
iron-sulfur centre
-
6.9 atoms of non-heme iron and 6.7 atoms of acid-labile sulfide per molecule of enzyme, iron-sulfur groups may participate in enzyme activity
iron-sulfur centre
-
one 4Fe-4S cluster in a single polypeptide chain of 723 amino acids, located near the periphery of the molecule
iron-sulfur centre
-
-
iron-sulfur centre
-
enzyme contains one 3Fe-4S cluster and three 4Fe-4S cluster
iron-sulfur centre
-
12.5-12.8 non-heme iron atoms and 8.7-12.1 acid-labile sulfur atoms per 172 kDa enzyme; molybdo-iron-sulfur protein
molybdenum bis-molybdopterin guanine dinucleotide
-
one bis-MGD cofactor in a single polypeptide chain of 723 amino acids, extends across the interior of the molecule interacting with residues from all 4 domains, catalytic molybdenum site is coordinated to two MGD cofactors, Cys140 and a water/hydroxo ligand
molybdenum cofactor
-
0.93 atoms of molybdenum per enzyme molecule, molybdenum seems to be a part of a low-molecular weight peptide, the Mo-cofactor, to which it may be bound by interaction with thiol groups
molybdenum cofactor
-
enzyme contains 1 mol of molybdenum cofactor per mol of enzyme, composed of 1 atom Mo and 1 mol MGD
molybdenum cofactor
-
-
molybdenum cofactor
-
-
molybdo-(bismolybdopterin)guanine dinucleotide
-
Mo-bis-MGD, NapA of the periplasmic nitrate reductase, assimilatory nitrate reductases
molybdo-bis(pyranopterin guanine dinucleotide)
P09152
-
-
molybdopterin guanine dinucleotide
-
NapA binds molybdopterin guanine dinucleotide derivative of the molybdenum cofactor
molybdopterin guanine dinucleotide
-
enzyme contains a GMP conjugate of the molybdopterin cofactor: molybdopterin guanine dinucleotide, molybdenum coordination environment in both Mo(VI) and Mo(IV) oxidation states
molybdopterin guanine dinucleotide
-
molybdopterin guanine dinucleotide is the organic moiety of the molybdenum cofactor, one mol MGD per mol of enzyme
molybdopterin guanine dinucleotide
-
enzyme contains molybdopterin guanine dinucleotide cofactor
NAD(P)H
-
assimilatory nitrate reductases
[4Fe-4S]-center
P09152
-
-
molybdopterin guanine dinucleotide
-
contains approximately 1.3 molybdopterin guanine dinucleotides per enzyme molecule
additional information
-
enzyme contains no FAD and FMN; non-heme enzyme
-
additional information
-
enzyme contains no cytochrome
-
additional information
-
no b-type cytochrome
-
additional information
-
non-heme enzyme
-
additional information
-
enzyme is free of spectroscopically detectable cytochrome
-
additional information
-
enzyme contains no cytochrome
-
additional information
-
absence of cytochrome b1 can be attributed to the isolation procedure, it is present up to gel filtration in Sephacryl 200 during purification; enzyme contains no cytochrome
-
additional information
-
napB and napC genes with two and four c-type cytochrome consensus heme-binding motifs
-
additional information
-
neither cytochrome nor flavin moiety is found in the purified preparation as judged from the absorption spectra
-
additional information
-
no cofactor: NADH
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe
-
NarG and NarH subunits of the respiratory nitrate reductases contain Fe-S clusters, NapA of the periplasmic nitrate reductase, assimilatory nitrate reductases
Fe
-
the molybdenum cofactor and the ironsulfur centre of NapA are attached in the cytoplasm by specific maturation systems prior to Holo-NapA export by the twin-arginine translocation (Tat) complex
Fe
-
the spectroscopic properties revealed the presence of iron-sulfur centers, presumably [4Fe-4S]- or [3Fe-4S]-type clusters
Fe
-
subunit NapG contains four [4Fe-4S] clusters, each ligated by four cysteine residues that are organized in a primary structure arrangement typical of polyferredoxins
Iron
-
enzyme contains iron-sulfur centres
Iron
-
enzyme contains 2 Fe atoms per enzyme molecule, non-heme iron protein
Iron
-
molybdo-iron-sulfur protein
Iron
-
molybdo-iron-sulfur protein; nitrate reductase I and II: 8 iron-sulfur groups, nitrate reductase I: additional 4 tightly bound non-heme iron atoms per enzyme molecule, nitrate reductase II: no tightly bound iron
Iron
-
contains iron
Iron
-
contains non-heme iron
Iron
-
6 atoms of non-heme iron and 12 mol of labile sulfide in 1 mol of purified enzyme
Iron
-
16 g-atoms of iron per mol of enzyme
Iron
-
6.9 atoms of non-heme iron per molecule of enzyme
Iron
-
15.4 mol iron per mol enzyme complex as cofactor
Iron
-
contains 12.5-12.8 non-heme iron atoms per 172 kDa enzyme
Iron
-, Q93HX3
non-heme iron and heme c, 5.4 mol iron per mol of enzyme
Iron
-
enzyme contains Fe-S clusters. NarB codes for a 219-amino-acid-residue iron Rieske protein.
Iron
-
the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA
Iron
-
non-heme iron
Iron
-
3Fe-4S cluster, cyclic voltammetry studies using enzyme protein films
Iron
-
contains approximately 14 Fe per enzyme molecule, [3Fe-4S]+ cluster, at least three types of [4Fe-4S] centers
iron-sulfur centre
-
enzyme contains iron-sulfur centres
iron-sulfur centre
-
enzyme contains 2 non-heme Fe atoms and 4 labile sulfide groups in acid medium per enzyme molecule
iron-sulfur centre
-
molybdo-iron-sulfur protein
iron-sulfur centre
-
molybdo-iron-sulfur protein; nitrate reductase I, MW 260000, abc2: 8 iron-sulfur groups per molecule of enzyme, which participate in electron transfer
iron-sulfur centre
-
6 atoms of non-heme iron and 12 mol of labile sulfide in 1 mol of purified enzyme
iron-sulfur centre
-
16 g-atoms of iron and 14 g-atoms of acid-labile sulfide per mol of enzyme
iron-sulfur centre
-
6.9 atoms of non-heme iron and 6.7 atoms of acid-labile sulfide per molecule of enzyme, iron-sulfur groups may participate in enzyme activity
iron-sulfur centre
-
one 4Fe-4S cluster in a single polypeptide chain of 723 amino acids, located near the periphery of the molecule
iron-sulfur centre
-
-
iron-sulfur centre
-
enzyme contains one 3Fe-4S cluster and three 4Fe-4S cluster
iron-sulfur centre
-
12.5-12.8 non-heme iron atoms and 8.7-12.1 acid-labile sulfur atoms per 172 kDa enzyme; molybdo-iron-sulfur protein
Mo
-
the exchange of the amino acid residue ligating the Mo atom from a cysteine (C181) to a serine results in a complete loss of nitrate reductase activity, underlining the importance of Mo complexation by sulphur
Mo
-
the molybdenum cofactor and the ironsulfur centre of NapA are attached in the cytoplasm by specific maturation systems prior to Holo-NapA export by the twin-arginine translocation (Tat) complex
Mo
-
the electron paramagnetic resonance spectrum of the purified enzyme revealed typical rhombic signals which were ascribed to Mo(V) in the Mo-molybdopterin complex. 0.33 mol Mo per mol of the 63000 Da polypeptide
Molybdenum
-
enzyme contains 1 Mo atom per enzyme molecule
Molybdenum
-
molybdenum containing iron-sulfur protein
Molybdenum
-
molybdenum containing iron-sulfur protein; nitrate reductase I, MW 260000, abc2: 0.24 atoms Mo per enzyme molecule, nitrate reductase II, MW 180000, 0.22 atoms Mo per enzyme molecule, Mo participates in electron transfer
Molybdenum
-
contains molybdenum
Molybdenum
-
4 molecules of molybdenum per enzyme molecule, 1 Mo is associated with each pair of subunits, large plus small, Mo interacts directly with the substrate
Molybdenum
-
molybdenoenzyme
Molybdenum
-
molybdenum center
Molybdenum
-
1 mol molybdenum per mol of enzyme
Molybdenum
-
molybdenoenzyme
Molybdenum
-
0.8 g-atom of molybdenum per mol of enzyme
Molybdenum
-
0.93 atoms of molybdenum per enzyme molecule, molybdenum seems to be a part of a low-molecular weight peptide to which it may be bound by interaction with thiol groups
Molybdenum
-
molybdenum-containing enzyme, catalytic molybdenum site is coordinated to two MGD cofactors, Cys140 and a water/hydroxo ligand
Molybdenum
-
0.8 mol Mo per mol enzyme complex as cofactor
Molybdenum
-
molybdenoenzyme
Molybdenum
-
molybdenum coordination environment in both Mo(VI) and Mo(IV) oxidation states, conserved Cys-181 of periplasmic enzyme is proposed to be part of Mo-binding site
Molybdenum
-
contains 0.49-0.85 molybdenum atoms per 172 kDa enzyme
Molybdenum
-, Q93HX3
0.83 mol per mol of enzyme
Molybdenum
-
enzyme contains molybdenum. When molybdenum concentrations are limiting, molybdenum is involved in the regulation of the expression of the nap genes: the ModA mutant lacks both the 90000 Da protein corresponding to the NapA component of nitrate reductase, and the membrane-bound 25000 Da c-type cytochrome NaC
Molybdenum
-
the diheme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. The plasticity of the complex contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA
Molybdenum
-
-
NaCl
-
0.17 M NaCl + 0.5 mM MgCl2 activates, 4.27 M NaCl + 0.5 mM MgCl2 inhibits
NaCl
-
the enzyme is activated in extreme saline conditions (2.0 M), inhibition above 2.0 M
Tungsten
-
0.06 mol tungsten per mol of enzyme complex
Molybdenum
-
contains approximately 0.8 Mo per enzyme molecule
additional information
-
NaCl activates not
additional information
-
no effect on enzyme activity by salts
additional information
-
no iron or cytochrome is found
additional information
-
Fe2+ and molybdate in growth medium promotes enzyme production
additional information
-
molybdenum, vanadium, and tungsten are not detected the enzyme complex and the 62000 Da cytochrome c
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-n-heptyl-4-hydroxyquinoline N-oxide
-
only effective as inhibitor with the three-subunit enzyme and duroquinol as substrate
ammonium sulfate
-
ammonium sulfate and other ammonium salts inhibit
azide
-
competitive inhibition; higher affinity for azide than for nitrate or chlorate
azide
-
strong inhibitor, competitive to nitrate; uncompetitive to reduced benzyl viologen, completely reversible inhibition
azide
-
azide-sensitive nitrate-reducing site of enzyme is located on the outer aspect of the cytoplasmic membrane; strong inhibitor, competitive to nitrate
azide
-
competitive to nitrate, non-competitive to benzyl viologen
azide
-
membrane-bound enzyme form is highly sensitive, but not periplasmic form
azide
-
competitive inhibition
azide
-
competitive inhibition
azide
-
1 mM, 68% loss of activity
azide
-
competitve with nitrate
azide
-
IC50 18.2-23.1 microM
azide
Halomonas sp.
-
-
azide
-
0.05 mM azide, more than 97% inhibition
azide
-
strong inhibition
bathophenanthroline
-
uncompetitive inhibition
bathophenanthroline-sulfonate
-
uncompetitive inhibition
bromate
-
competitive inhibitor, 1 mM, 50% inhibition
Chlorate
-
competitive inhibitor
-
Chlorate
-
1 mM, 50% inhibition; competitive inhibitor
-
Chlorate
-
20 mM chlorate inhibits nitrate reduction by 10% in the cell-free lysate; 20 mM chlorate inhibits nitrate reduction by 67% in the whole-cell lysate
-
cyanide
-
mixed non-competitive to nitrate, only partly reversible inhibition, modification of a persulfide group in the vicinity of the Mo atom
cyanide
-
1 mM, 81% inhibition
cyanide
-
1 mM, about 80% inhibition
cyanide
-
reduced enzyme is more sensitive at pH 7.2 than at pH 10.5, at pH 10.5 reversible enzyme-cyanide complexes are formed with reduced enzyme, nitrate protects reduced enzyme for inactivation, oxidized enzyme is less sensitive, kinetics of inactivation
cyanide
-
non-competitive inhibition, reduces Vmax of enzyme by 3fold
cyanide
-
1 mM, 76% loss of activity
cyanide
-
IC50 13.4-21.4 microM
cyanide
Halomonas sp.
-
-
Dithiol
-
0.1 mM, 95% inhibition
Dithionite
-
1 mM, 24% loss of activity
dithiothreitol
-
inactivates at 1 mM
EDTA
-
1 mM, 22% loss of activity
ferricyanide
-
at pH 10.5 the as prepared enzyme is inactivated
IO3-
-
1 mM, 40% inhibition
KClO4
-
1 mM, 33% inhibition
Mepacrine
-
1 mM, 40% inhibition
NaCl
-
0.17 M NaCl + 0.5 mM MgCl2 activates, 4.27 M NaCl + 0.5 mM MgCl2 inhibits
NaCN
-
0.04 mM, complete inhibition
NaN3
-
0.04 mM, 59% inhibition
NH4HCO3
-
3.87 mM, complete inhibition
Nitrofurantoin
-
0.3 mM nitrofurantoin inhibits nitrate reduction by 19.5% in the whole-cell lysate
o-phenanthroline
-
3 mM, 25% inhibition
oxygen
-
inhibition of activity in intact cells in presence of oxygen, membrane-bound form is inhibited by 90% under aerobic conditions
oxygen
-
oxygen reversibly inhibits nitrate reduction by spores but not by spore extracts, suggesting that nitrate transport might be the target of oxygen inhibition
p-chloromercuribenzoate
-
above 0.1 mM non-competitive inhibition
p-chloromercuribenzoate
-
2 mM, 60% inhibition
Sulfide
-
more strong inhibition of dithionite-reduced enzyme than of oxidized enzyme, nearly complete restoration of activity by 5 mM dithiothreitol, formation of iron-sulfide complexes
-
Sulfide
-
inactivates in absence of cyanide
-
Thiocyanate
-
non-competitive to nitrate, completely reversible inhibition
Thiocyanate
-
1.5 mM, 75% inhibition
Thiocyanate
-
20 mM thiocyanate, more than 97% inhibition
metronidazole
-
2 mM metronidazole inhibits nitrate reduction by 6.7% in the whole-cell lysate
additional information
-
NAP activity in intact cells is insensitive towards ammonium, no inactivation by oxygen
-
additional information
-
not inhibitory: ammonium
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
deoxycholate
-
activates
ferricyanide
-
enzyme as prepared is slowly activated at pH 7.2 over 250% of the original activity, dependent on ferricyanide concentration, little activation at pH 9.5
isopentenyladenine
C3U5B4
nitrate reductase expression and activity in both roots and shoots of pineapple are significantly enhanced by isopentenyladenine
isopentenyladenine riboside
C3U5B4
nitrate reductase expression and activity in both roots and shoots of pineapple are significantly enhanced by isopentenyladenine riboside
K3Fe(CN)6
-
the enzyme, inactive in vivo, may be reactivated in vitro by oxidation with K3Fe(CN)6
nitrate
-
slightly
-
nitrate
-
the 230000 Da activity-band increases severalfold, up to h 4 of growth on 2 mM nitrate, however, during the next 2 h, the nitrate reductase activity of this complex decreases remarkably
-
nitrite
-
the activity of the 125000 Da complex increases strikingly from 0.1 mM to 1 mM nitrite added, however, within the higher range of available nitrite, the intensity of this form decreases dramatically, whereas the activity of the 140000 Da band starts to grow in strength
p-chloromercuribenzoate
-
enhances enzyme activity at 0.1 mM and lower concentrations
zeatin
C3U5B4
nitrate reductase expression and activity in both roots and shoots of pineapple are significantly enhanced by zeatin
zeatin riboside
C3U5B4
nitrate reductase expression and activity in both roots and shoots of pineapple are significantly enhanced by zeatin riboside
KNO3
-
10 mM, up to 4fold activation
additional information
-
4fold activation by heating to 75C for 75 min
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0022
-
benzyl viologen
-
pH 7.4, 30C
0.0029
-
benzyl viologen
-
pH 7.4, 30C, enzyme activated by heating
0.138
-
Chlorate
-
pH 7.9, 40C
-
0.14
-
Chlorate
-
-
-
0.47
-
Chlorate
-
with duroquinol as electron donor
-
5
-
Chlorate
-
-
-
0.0032
-
nitrate
-, Q93HX3
25C
-
0.013
-
nitrate
-
with duroquinol or reduced methyl viologen as electron donor
-
0.032
-
nitrate
-
pH 7.2
-
0.058
-
nitrate
-
-
-
0.079
-
nitrate
-
in presence of 2.0 M NaCl
-
0.1
-
nitrate
-
-
-
0.11
-
nitrate
-
-
-
0.11
-
nitrate
-
pH 7.9, 40C
-
0.12
-
nitrate
-
pH 7
-
0.2
-
nitrate
-
-
-
0.24
-
nitrate
-
20C, after growth on 0.003 mM molybdate
-
0.283
-
nitrate
-
with reduced methyl viologen as electron donor
-
0.29
-
nitrate
-
pH 7.4, 30C
-
0.31
-
nitrate
-
pH 7.4, 30C, enzyme activated by heating
-
0.38
-
nitrate
-
recombinant enzyme with N-terminal His-tag, pH 10.25, 30C
-
0.47
-
nitrate
-
-
-
0.6
-
nitrate
-
-
-
0.67
-
nitrate
-
-
-
0.8
-
nitrate
-
oxidized enzyme
-
0.82
-
nitrate
-
-
-
1.3
-
nitrate
-
-
-
3.91
-
nitrate
-
20C, after growth on 0.1 mM tungstate
-
5
-
nitrate
-
reduced enzyme
-
0.0002
-
reduced benzyl viologen
-
-
0.057
-
reduced benzyl viologen
-
-
0.07
-
reduced benzyl viologen
-
nitrate as substrate
0.12
-
reduced benzyl viologen
-
chlorate as substrate
1.6
-
reduced benzyl viologen
-
nitrate as substrate
0.8
-
reduced methyl viologen
-
nitrate as substrate
1.5
-
reduced methyl viologen
-
chlorate as substrate
0.25
-
methyl viologen
-
-
additional information
-
additional information
-
apparent Km for reduction of nitrate by the respiratory chain is 10fold less than that when the reductant is reduced benzyl viologen
-
additional information
-
additional information
-
native enzyme, biphasic kinetics for nitrate, Km (I), 0.12 mM, Km (II), 4.17 mM, recombinant enzyme with C-terminal His-tag, biphasic kinetics with Km (I) 0.20 mM, Km (II) 1.78 mM, pH 10.25, 30C
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1350
-
Chlorate
-
at 75C
-
2.5
-
nitrate
-, Q93HX3
25C
-
71
-
nitrate
-
in absesence of NaCl, per mol of 63000 Da polypeptide
-
145
-
nitrate
-
in presence of 2.0 M NaCl, per mol of 63000 Da polypeptide
-
1160
-
nitrate
-
at 75C
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00013
-
azide
-
nitrate as substrate
0.0002
-
azide
-
when assayed spectrophotometrically
0.0003
-
azide
-
nitrate as substrate
0.0011
-
azide
-
chlorate as substrate
0.002
0.005
azide
-
when assayed manometrically
0.002
-
azide
-
nitrite as substrate
0.002
-
azide
-
pH 7.4, 30C, substrate nitrate
0.01
-
azide
-
reduced benzyl viologen as substrate
0.0173
-
azide
-
reduced benzyl viologen as substrate
0.025
-
azide
-
pH 7.4, 30C, substrate benzyl viologen
0.5
-
bathophenanthroline
-
nitrate as substrate
0.8
-
bathophenanthroline
-
reduced benzyl viologen as substrate
1.3
-
bathophenanthroline-sulfonate
-
nitrate as substrate
2.4
-
bathophenanthroline-sulfonate
-
reduced benzyl viologen as substrate
1.3
-
Chlorate
-
-
-
1.7
-
Chlorate
-
-
-
0.044
-
cyanide
-
at pH 10.5, reduced enzyme
0.3
-
cyanide
-
nitrate as substrate
0.16
-
Sulfide
-
nitrate as substrate, reduced enzyme
-
0.28
-
Sulfide
-
nitrate as substrate, oxidized enzyme
-
1.4
-
Thiocyanate
-
nitrate as substrate
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0182
0.0231
azide
-
IC50 18.2-23.1 microM
0.036
-
azide
Halomonas sp.
-
-
0.0134
0.0214
cyanide
-
IC50 13.4-21.4 microM
0.11
-
cyanide
Halomonas sp.
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0003
-
-
nitrate, 10 mM NH4+, NADPH, aerobic
0.0057
-
-
nitrate, medium without nitrogen, NADPH, aerobic
0.0129
-
-
nitrate, 10 mM NO3-, NADPH, aerobic
0.0186
-
-
nitrate, 10 mM NH4+, methyl viologen, aerobic; nitrate, 10 mM NH4+, NADPH, anaerobic
0.02
0.04
-
rate of physiological reduction, lower than that obtained with reduced benzyl viologen
0.02
-
-
nitrate, medium without nitrogen, methyl viologen, aerobic
0.066
-
-
nitrate, medium without nitrogen, NADPH, anaerobic
0.0705
-
-
nitrate, 10 mM NO3-, methyl viologen, aerobic; nitrate, 10 mM NO3-, NADPH, anaerobic
0.0754
-
-
nitrate, 10 mM NH4+, methyl viologen, anaerobic
0.2659
-
-
nitrate, medium without nitrogen, methyl viologen, anaerobic
0.342
-
-
methyl viologen as electron donor, aerobic growth conditions, assay in intact cells
0.39
-
-
nitrate/nitrite reductase complex
0.423
-
-
nitrate, 10 mM NO3-, methyl viologen, anaerobic
0.523
-
-
benzyl viologen as electron donor, aerobic growth conditions, assay in intact cells
1.407
-
-
benzyl viologen as electron donor, anaerobic growth conditions, assay in intact cells
2.018
-
-
methyl viologen as electron donor, anaerobic growth conditions, assay in intact cells
2.157
-
-
methyl viologen as electron donor, microaerobic growth conditions, assay in intact cells
2.264
-
-
benzyl viologen as electron donor, microaerobic growth conditions, assay in intact cells
2.63
-
-
enzyme in cell-free extract
24.5
-
-
nitrate reductase I
35
-
P85098 and P85097
after 76fold purification
39.1
-
-
nitrate reductase II
76.19
-
-
-
160
-
-
at 30C, both enzyme forms, reduced benzyl viologen as reductant
229
-
-
at 30C
250
-
Halomonas sp.
-
-
326
-
-
nitrate as substrate, at 75C
378
-
-
chlorate as substrate, at 75C
2530
-
-
pH 7.4, 30C
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
-
-
nitrate as substrate
6.4
-
-
chlorate as substrate
6.8
-
-
broad pH-optimum from pH 5.8 to pH 7.1 with maximum at pH 6.8
7
-
-
activity assay
7
-
Halomonas sp.
-
-
7.1
-
-
nitrate as substrate
7.2
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
activity assay; activity assay; activity assay; activity assay; activity assay
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
activity assay
32
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
activity assay; activity assay; activity assay; activity assay; activity assay
56
-
-
presence of 0.5 mM MgCl2
70
-
-
at 3.4 M NaCl
73
-
-
presence of 2 M KCl
75
-
-
optimum of 5 min reaction
75
-
Halomonas sp.
-
-
80
-
-
assay at
85
-
-
presence of 4.27 M NaCl
95
-
-
highest activity at or above
additional information
-
-
temperature optimum is a function of both: the concentration and the specific cation present, increasing NaCl and KCl concentrations result in an increase in the maximal activity at higher temperatures
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
80
Halomonas sp.
-
maximal activity
additional information
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.1
-
-
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
respiratory nitrate reductase Nar-1 is functional exclusively in spores and displays a tight coupling between nitrite production and the activity of the cytoplasmically oriented Nar-1 enzyme. Nar-1 is synthesized during sporulation and remains in a latently active state throughout the lifetime of the spore
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
NarG; NarH; NarJ
Manually annotated by BRENDA team
-
NarG and NarH subunits of the respiratory nitrate reductases
Manually annotated by BRENDA team
-
bound to cytoplasmic membrane
-
Manually annotated by BRENDA team
-
beta-subunit is located at the internal surface of the cytoplasmic membrane, alpha-subunit is similarly located at the cytoplasmic face of the membrane
-
Manually annotated by BRENDA team
-
in cell-membrane fraction
-
Manually annotated by BRENDA team
-
bound to cytoplasmic membrane
-
Manually annotated by BRENDA team
-
located solely on the cytoplasmic surface of the membrane
-
Manually annotated by BRENDA team
-
the 2 subunits are localized on the cytoplasmic side of the membrane
-
Manually annotated by BRENDA team
-
NarC, a cytochrome c, is required for the attachment of the alpha subunit to the cytoplasmic membrane
-
Manually annotated by BRENDA team
Bacillus licheniformis S244
-
located solely on the cytoplasmic surface of the membrane; the 2 subunits are localized on the cytoplasmic side of the membrane
-
-
Manually annotated by BRENDA team
Escherichia coli A1002
-
bound to cytoplasmic membrane
-
-
Manually annotated by BRENDA team
Escherichia coli EMG
-
beta-subunit is located at the internal surface of the cytoplasmic membrane, alpha-subunit is similarly located at the cytoplasmic face of the membrane
-
-
Manually annotated by BRENDA team
Escherichia coli K12
-
bound to cytoplasmic membrane; bound to cytoplasmic membrane
-
-
Manually annotated by BRENDA team
Escherichia coli RK7
-
bound to cytoplasmic membrane
-
-
Manually annotated by BRENDA team
Bradyrhizobium sp. USDA 3045
-
-
-
Manually annotated by BRENDA team
-
alpha- and beta-subunits are exposed on the cytoplasmic surface of the cytoplasmic membrane, they are peripheral polypeptides that are attached to the membrane presumably via the gamma-subunit, which is embedded to the membrane
-
Manually annotated by BRENDA team
-
incorporation into the cytoplasmic membrane, enzyme site that oxidizes FMNH2 is located on the cytoplasmic aspect of cytoplasmic membrane
-
Manually annotated by BRENDA team
-
nitrate reductase spans the cytoplasmic membrane and is vectorial, reducing nitrate on the outer aspect of the membrane with 2 H+ and 2 electrons that have crossed from the inner aspect of the membrane
-
Manually annotated by BRENDA team
-
transmembrane protein of cytoplasmic membrane
-
Manually annotated by BRENDA team
Escherichia coli A1004a
-
incorporation into the cytoplasmic membrane, enzyme site that oxidizes FMNH2 is located on the cytoplasmic aspect of cytoplasmic membrane
-
-
Manually annotated by BRENDA team
Escherichia coli EMG-2
-
nitrate reductase spans the cytoplasmic membrane and is vectorial, reducing nitrate on the outer aspect of the membrane with 2 H+ and 2 electrons that have crossed from the inner aspect of the membrane
-
-
Manually annotated by BRENDA team
-
membrane-bound; solubilized from membrane
Manually annotated by BRENDA team
-
in membrane fraction
Manually annotated by BRENDA team
-
a periplasmic enzyme is expressed under both aerobic and anaerobic conditions and a membrane-bound enzyme is synthesized only under anaerobic conditions
Manually annotated by BRENDA team
Halomonas sp.
-
-
Manually annotated by BRENDA team
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
NarI; NarK; nitrate reductase encoded by the narGHJI operon; nitrate reductase encoded by the narGHJI operon; nitrate reductase encoded by the narGHJI operon; nitrate reductase encoded by the narGHJI operon; nitrate reductase encoded by the narGHJI operon
Manually annotated by BRENDA team
-
in the synthesis of NRT, a NarCI membrane complex and a soluble NarGJH complex are synthesized in a first step. In a second step, both complexes interact at the cytoplasmic face of the membrane, where the enzyme is subsequently activated with the concomitant conformational change and release of the NarJ chaperone from the mature enzyme. NarJ is required for the attachment of the thermophilic enzyme to the membrane
Manually annotated by BRENDA team
-
NarI subunit of the respiratory nitrate reductases
Manually annotated by BRENDA team
-
the iron-sulfur protein NapG forms a complex with NapH in the membrane but is detected in the periplasmic cell fraction in the absence of NapH
Manually annotated by BRENDA team
Bradyrhizobium sp. USDA 3045
-
;
-
Manually annotated by BRENDA team
Enterobacter cloacae IFO 12935
-
membrane-bound
-
Manually annotated by BRENDA team
Escherichia coli K12
-
in membrane fraction; membrane-bound; membrane-bound
-
Manually annotated by BRENDA team
Escherichia coli X5119
-
membrane-bound
-
Manually annotated by BRENDA team
Gordonia alkanivorans S7, Halomonas sp. AGJ1-3
-
-
-
Manually annotated by BRENDA team
Marinobacter hydrocarbonoclasticus 617
-
bound to
-
Manually annotated by BRENDA team
Paracoccus pantotrophus LMD82.5
-
a periplasmic enzyme is expressed under both aerobic and anaerobic conditions and a membrane-bound enzyme is synthesized only under anaerobic conditions
-
Manually annotated by BRENDA team
-
a periplasmic enzyme is expressed under both aerobic and anaerobic conditions and a membrane-bound enzyme is synthesized only under anaerobic conditions
-
Manually annotated by BRENDA team
-
periplasmic nitrate reductases
-
Manually annotated by BRENDA team
-
in order to catalyse nitrate reduction Epsilonproteobacteria encode the periplasmic nitrate reductase system (Nap) whereas genes encoding the subunits of the membrane-bound nitrate reductase complex (NarGHI) are absent
-
Manually annotated by BRENDA team
-
the iron-sulfur protein NapG forms a complex with NapH in the membrane but is detected in the periplasmic cell fraction in the absence of NapH
-
Manually annotated by BRENDA team
Azospirillum brasilense SP245, Bradyrhizobium japonicum USDA110
-
-
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus LMD82.5
-
a periplasmic enzyme is expressed under both aerobic and anaerobic conditions and a membrane-bound enzyme is synthesized only under anaerobic conditions
-
-
Manually annotated by BRENDA team
Paracoccus pantotrophus M-6
-
-
-
-
Manually annotated by BRENDA team
-
it may exist an additional enzyme that associates the soluble enzyme with the cytoplasmic membrane
-
Manually annotated by BRENDA team
-
narC::kat mutant with soluble NarG
-
Manually annotated by BRENDA team
Pseudomonas fluorescens YT101
-
membrane-bound
-
Manually annotated by BRENDA team
additional information
-
NapG and NapH proteins form a membrane-bound protein complex that is likely to catalyse menaquinol oxidation and electron transport to the periplasmic NapAB nitrate reductase complex
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23000
-
-
enzyme form predominating in the membrane fraction, SDS-PAGE
26000
-
-
gel filtration
28690
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
calculated, NarJ
46060
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
calculated, NarK
59000
-
P85098 and P85097
two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE
60840
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
calculated, NarH
65000
-
P85098 and P85097
two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE
125000
-
-
enzyme form with remarkably increased activity, SDS-PAGE
130000
-
Halomonas sp.
-
determined by SDS-PAGE
137000
-
P85098 and P85097
purified homogenous alpha subunit, non-denaturing PAGE
140000
-
-
active enzyme form, SDS-PAGE
141400
-
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
calculated, NarG
165000
-
-
mean value, real value between 155000 Da and 175000 Da, PAGE
176000
-
-
analytical ultracentrifugation
176000
-
-
PAGE
180000
220000
P85098 and P85097
purified native enzyme, gel filtration
180000
-
-
nitrate reductase II, monomeric form, gel filtration
180000
-
-
gel filtration of urea-treated enzyme
190000
-
-
in the nitrate-fed cells, the 190000 Da form is the most abundant, SDS-PAGE
196000
-
-
always present in a monomeric form, PAGE
200000
-
-
8.5 S monomeric state, gel filtration
200000
-
-
in presence of deoxycholate, dissociated form, gel filtration
208000
-
-
gel filtration
214000
-
-
three-subunit complex, calculated as the sum of the MWs of the subunits
220000
-
-
monomer form of the enzyme, analytical ultracentrifugation in presence of 0.2% deoxycholate
230000
-
P85098 and P85097
non-denaturing PAGE
235000
-
-
sucrose density gradient sedimentation
240000
-
-
gel filtration
260000
-
-
nitrate reductase I, abc2, monomeric form, gel filtration
265000
-
-
nitrate reductase from aerobic variant, estimated by gel filtration on a Toyopearl HW-55 column
290000
-
-
gel filtration; one of the two enzyme forms with different subunit compositions
290000
-
-
gel filtration
320000
-
-
in absence of deoxycholate, associated form, gel filtration
355000
-
-
nitrate reductase from anaerobic variant, estimated by gel filtration on a Toyopearl HW-55 column
400000
-
-
13.9 S dimeric state, gel filtration
620000
-
-
gel filtration; one of the two enzyme forms with different subunit compositions
620000
-
-
gel filtration
720000
-
-
gel filtration
773000
-
-
analytical ultracentrifugation
880000
-
-
associated, probably tetrameric, form of enzyme
1000000
-
-
-
1060000
-
-
nitrate reductase I, (abc2)4, tetrameric form, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 150000 alpha + x * 60000 beta + x * 20000 gamma, that is the apoprotein of cytochrome c-556, alpha-subunit is involved in catalysis
?
-
x * 150000 alpha + x * 67000 beta1 + x * 65000 beta2, molar ratio alpha:beta1 + beta2 is 1:1, SDS-PAGE
?
-
an additional 20 kDa subunit is present in heme-containing enzyme; x * 150000 alpha + x * 67000 beta1 + x * 65000 beta2, molar ratio alpha:beta1 + beta2 is 1:1, SDS-PAGE
?
-
x * 150000 alpha + x * 59000 beta
?
-
x * 150000 alpha + x * 60000 beta + x * 19000 gamma, alpha-subunit with catalytic function containing molybdenum cofactor and non-heme iron, beta-subunit is possibly involved in membrane binding, gamma-subunit is found in some preparations and is a b-type cytochrome
?
-
x * 150000 + x * 58000 + x * 42000, SDS-PAGE
?
-
x * 91000 + x * 17000, SDS-PAGE
?
-
x * 62000 + x * 52000 + x * 36000 + x * 16000, SDS-PAGE
?
-, Q93HX3
x * 17000 + x * 86000, SDS-PAGE
?
-
x * 83400, deduced from gene sequence, x * 82500, SDS-PAGE, recombinant enzyme
?
-
napA encodes the catalytic subunit, the napB gene product is a soluble dihaem c and the napC gene product is a membrane-anchored tetrahaem c-type cytochrome, napE encodes a transmembrane protein of unknown function, the napD gene product is a soluble protein which is assumed to play a role in the maturation of NapA
?
-
x * 118000 + x * 62000, SDS-PAGE
?
P85098 and P85097
x * 59000, two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE; x * 65000, two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE
?
-
x * 125000, enzyme form with remarkably increased activity, SDS-PAGE; x * 140000, active enzyme form, SDS-PAGE; x * 190000, in the nitrate-fed cells, the 190000 Da form is the most abundant, SDS-PAGE; x * 23000,enzyme form predominating in the membrane fraction, SDS-PAGE
?
Bradyrhizobium japonicum USDA110
-
napA encodes the catalytic subunit, the napB gene product is a soluble dihaem c and the napC gene product is a membrane-anchored tetrahaem c-type cytochrome, napE encodes a transmembrane protein of unknown function, the napD gene product is a soluble protein which is assumed to play a role in the maturation of NapA
-
?
Bradyrhizobium sp. USDA 3045
-
x * 125000, enzyme form with remarkably increased activity, SDS-PAGE; x * 140000, active enzyme form, SDS-PAGE; x * 190000, in the nitrate-fed cells, the 190000 Da form is the most abundant, SDS-PAGE; x * 23000,enzyme form predominating in the membrane fraction, SDS-PAGE; x * 59000, two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE; x * 65000, two bands of 65 kDa and 59 kDa are obtained as beta-subunit after purification, SDS-PAGE
-
?
Escherichia coli A1002
-
an additional 20 kDa subunit is present in heme-containing enzyme; x * 150000 alpha + x * 67000 beta1 + x * 65000 beta2, molar ratio alpha:beta1 + beta2 is 1:1, SDS-PAGE
-
?
Escherichia coli EMG
-
x * 150000 alpha + x * 59000 beta
-
?
Escherichia coli K12
-
an additional 20 kDa subunit is present in heme-containing enzyme; x * 150000 alpha + x * 60000 beta + x * 19000 gamma, alpha-subunit with catalytic function containing molybdenum cofactor and non-heme iron, beta-subunit is possibly involved in membrane binding, gamma-subunit is found in some preparations and is a b-type cytochrome; x * 150000 alpha + x * 67000 beta1 + x * 65000 beta2, molar ratio alpha:beta1 + beta2 is 1:1, SDS-PAGE; x * 150000 alpha + x * 67000 beta1 + x * 65000 beta2, molar ratio alpha:beta1 + beta2 is 1:1, SDS-PAGE; x * 150000 + x * 58000 + x * 42000, SDS-PAGE
-
?
Escherichia coli X5119
-
x * 150000 alpha + x * 60000 beta + x * 19000 gamma, alpha-subunit with catalytic function containing molybdenum cofactor and non-heme iron, beta-subunit is possibly involved in membrane binding, gamma-subunit is found in some preparations and is a b-type cytochrome
-
?
-
x * 17000 + x * 86000, SDS-PAGE
-
?
Synechococcus sp. RF-1
-
x * 83400, deduced from gene sequence, x * 82500, SDS-PAGE, recombinant enzyme
-
dimer
-
1 * 117000 + 1 * 57000, nitrate reductase II, SDS-PAGE
dimer
-
alpha,beta, 1 * 120000 + 1 * 60000, alpha subunit: catalytic subunit, beta subunit: a membrane attachment protein, SDS-PAGE
dimer
-
alpha,beta, 1 * 150000 + 1 * 44000, SDS-PAGE
dimer
-
alpha,beta, 1 * 150000 + 1 * 57000, SDS-PAGE
dimer
Bacillus licheniformis S244
-
alpha,beta, 1 * 150000 + 1 * 57000, SDS-PAGE; alpha,beta, 1 * 150000 + 1 * 57000, SDS-PAGE
-
heterodimer
-
-
heterodimer
-
assimilatory nitrate reductases from Klebsiella pneumoniae and Rhodobacter capsulatus, catalytic subunit 90-105 kDa, small subunit approximately 45 kDa; periplasmatic nitrate reductases, large subunit 80-90 kDa, small subunit appoximately 17 kDa, NapA and NapB assemble to NabAB
heterotetramer
-
-
heterotrimer
-
respiratory nitrate reductases composed of the subunits NarG, 112-140 kDa, NarH, 52-64 kDa and NarI, 19-25 kDa
hexadecamer
-
4 * 117000 + 4 * 57000 + 8 * 52000, nitrate reductase II, SDS-PAGE
monomer
-
the simplest of the soluble nitate reductases
monomer
Halomonas sp.
-
-
monomer
-
assimilatory nitrate reductases from Azotobacter vinelandii and Cyanobacteria, 75-105 kDa; periplasmatic nitrate reductase of Desulfovibrio desulfuricans
multimer
-
x * 103000, x * 53000, x * 25000, SDS-PAGE
multimer
Gordonia alkanivorans S7
-
x * 103000, x * 53000, x * 25000, SDS-PAGE
-
octamer
-
4 * 142000 + 4 * 58000, subunits are probably associated in form of a double tetrahedron, SDS-PAGE
octamer
Escherichia coli K12, Escherichia coli RK7
-
4 * 142000 + 4 * 58000, subunits are probably associated in form of a double tetrahedron, SDS-PAGE
-
tetramer
-
1 * 117000 + 1 * 57000 + 2 * 52000, nitrate reductase I with subunit structure abc2, 52 kDa subunit may have structural function, SDS-PAGE
tetramer
-
4 * 63000
trimer
-
alpha,beta,gamma, 1 * 127000 + 1 * 61000 + 1 * 21000, SDS-PAGE
trimer
-
1 * 100000 + 1 * 60000 + 1 * 31000
trimer
-
1 * 130000 + 1 * 52000 + 1 * 32000, SDS-PAGE
trimer
-
1 * 136000 + 1 * 65000 + 1 * 20000, SDS-PAGE
trimer
Marinobacter hydrocarbonoclasticus 617
-
1 * 136000 + 1 * 65000 + 1 * 20000, SDS-PAGE
-
trimer
Paracoccus denitrificans NCIB 8944
-
alpha,beta,gamma, 1 * 127000 + 1 * 61000 + 1 * 21000, SDS-PAGE
-
monomer
Halomonas sp. AGJ1-3
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-
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additional information
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enzyme is a heterotetrameric complex of subunits NarC/NarI/NarG/NarH. In the synthesis of enzyme, a NarCI membrane complex and a soluble NarGJH complex are synthesized in a first step. In a second step, both complexes interact at the cytoplasmic face of the membrane, where the enzyme is subsequently activated with the concomitant conformational change and release of the NarJ chaperone from the mature enzyme
additional information
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the iron-sulfur protein NapG forms a complex with NapH in the membrane but is detected in the periplasmic cell fraction in the absence of NapH
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
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NapB is characterized by a N-terminal signal peptide, cleavage site is predicted to be between two alanine residues at positions 25 and 26
proteolytic modification
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NapB is characterized by a N-terminal signal peptide, cleavage site is predicted to be between two alanine residues at positions 25 and 26
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no glycoprotein
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-
no glycoprotein
Bacillus licheniformis S244
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-
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additional information
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no proteolytic processing at the N-terminal end except for removal of N-formylmethionine
additional information
Escherichia coli K12, Escherichia coli X5119
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no proteolytic processing at the N-terminal end except for removal of N-formylmethionine
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Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapor diffusion method. Structure of proteolyzed form of recombinant NapB at 1.25 A resolution
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crystal structure determined at a resolution of 3.2 A
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pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
10
-
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
immobilized enzyme more stable at 6C than at 23C
20
-
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24 h, complete loss of activity
20
-
-
labile during prolonged incubation, after growth on tungstate
23
-
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immobilized enzyme more stable at 6C than at 23C
25
-
-
stable for mor than 30 h
50
-
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1 h, enzyme concentration: 0.1 mg per ml, no inhibition
50
-
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20 h, stable up to
50
-
-
stable up to, after growth on molybdate
50
-
-
90 min, stable
60
-
-
after 10 min and 5 h same activity observed, remarkably stable
60
-
-
20 h, 15% loss of activity
65
-
-
10 min, stable
80
-
-
0.17 M NaCl: 90% loss of activity after 1 min, 0.85 M NaCl: 50% loss of activity after 7 min, 4.27-5.31 M NaCl: no loss of activity after 15 min, high salt concentrations protect enzyme against heat inactivation at 80C due to a tighter, more stable configuration
100
-
-
half-life of 1.5 h, half-life within cell-membranes is 6 h, lipid environment stabilizes
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
deoxycholate stabilizes
-
nitrate reductase II, which lacks the 52 kDa subunit, is much more labile than nitrate reductase I, deoxycholate stabilizes nitrate reductase II
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sucrose stabilizes
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freezing rapidly inactivates enzyme at a concentration of 0.1 mg per ml, 0.1 mM dithiothreitol stabilizes
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immobilized enzyme more labile than free enzyme
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slow freezing inactivates, but rapid freezing in liquid N2 and thawing at room temperature can be repeated 10 times without effect on enzyme activity, when reduced benzyl viologen is used as reductant
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NaCl protects against heat inactivation, 4.27-5.31 M NaCl
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, aerobic or anaerobic storage, absence of deoxycholate: per 24 h, 30% inactivation, presence of 0.2% deoxycholate: per 24 h, 10% inactivation
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20C, 0.07 M imidazole buffer, pH 8.1, 24 h, nitrate reductase I: 45% loss of activity, probably due to loss of 52 kDa subunit and conversion to nitrate reductase II, nitrate reductase II: 95% loss of activity
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4C, 0.07 M imidazole buffer, pH 8.1, 24 h, nitrate reductase I: 10% loss of activity, nitrate reductase II: 35% loss of activity
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5C, 0.1 M Tris-HCl buffer, pH 8.8, 10% sucrose, 24 h, 10% loss of activity, without sucrose: 75% loss of activity
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4C, phosphate buffer, pH 7.2 or Tris-HCl buffer, pH 8.0, enzyme concentration less than 0.5 mg/ml: half live is 5 days under strict anaerobic conditions and 3 days in air, enzyme concentration above 10 mg/ml: under argon, 20 days, no loss of activity
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4C, prolonged storage, stable, when assayed with reduced benzyl viologen as reductant
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liquid N2 temperature, 6 months, stable
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4C, 3-4 weeks, remains active
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-70C, in glycerol, stable for at least 3 months
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room-temperature, many weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
85fold purification
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ammonium sulfate precipitation
-
ammonium sulfate precipitation, Macro-Prep High Q column chromatography, HiTrap Phenyl FF column chromatography, Sephadex G-25 gel filtration, and Sephacryl S-300 gel filtration
P85098 and P85097
100fold purification
-
2 forms: nitrate reductase I, nitrate reductase II
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2 forms: nitrate reductase I: 36.6fold purification, nitrate reductase II: 58.4fold purification
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112fold purification
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134fold purification
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140fold purification
-
2 enzyme forms with different subunit compositions
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strain X5119
-
the cell extract is centrifuged and the supernatant is used as source for the nitrate reductase
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53fold purification, alphabeta enzyme, cytochrome b1 is present up to gel filtration in Sephacryl 200 during purification
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partial purification of the nitrate/nitrite reductase complex
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partial purification
-
40fold purification
-
using non-denaturating preparative electrophoresis in 7.5% polyacrylamide gel with constant buffer elution
Halomonas sp.
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gamma-subunit of enzyme is lost during gel filtration purification, resulting in a cytochrome-free enzyme; partial
-
56fold purification
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purification of the catalytic alpha-subunit of nitrate reductase A
-
137fold purification
-
120fold purification
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His-tagged enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
napABC genes, encoding periplasmic nitrate reductase, are isolated and sequenced, NapB has 160 amino acides, NapC with 206 amino acids and a hydrophobic membrane-spanning domain near its N-terminus
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cloning of the narG gene, encoding the large alpha-subunit gene of enzyme, nucleotide sequence of part of nar DNA and sequence of N-terminal 147 amino acids of the alpha-subunit
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the membrane-bound nitrate reductase genes, nar genes, are cloned into the p-SCRIPT and pGEM-T vector for sequencing; the membrane-bound nitrate reductase genes, nar genes, are cloned into the p-SCRIPT and pGEM-T vector for sequencing; the membrane-bound nitrate reductase genes, nar genes, are cloned into the p-SCRIPT and pGEM-T vector for sequencing; the membrane-bound nitrate reductase genes, nar genes, are cloned into the p-SCRIPT and pGEM-T vector for sequencing; the membrane-bound nitrate reductase genes, nar genes, are cloned into the p-SCRIPT and pGEM-T vector for sequencing
-, Q6GUE2, Q6GUE3, Q6GUE4, Q6GUE5, Q6GUE6
construction of transcriptional fusion constructs carrying 5' truncations and generation of individual single-point mutations in the full-length promotor sequence, generating full-length promoter fragments harbouring lesions
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construction of napKEFD-lacZ translational gene fusions, dissection of the upstream region of napK of a nap-lacZ fusion plasmid, construction of the napC::omega-Smr/Spr insertion strain
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NarC, a 27 kDa membrane cytochrome c, is encoded as the first gene of the narCGHJIK1K2 operon for nitrate respiration and plays an essential role in the synthesis of active enzyme and for the attachment of enzyme to the membrane, sequence of narC, NarG is unable to bind to the cytoplasmic membrane in absence of NarC
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C181S
-
complete loss of nitrate reductase activity; inactive mutant enzyme
D196G
-
complete loss of nitrate reductase activity; inactive mutant enzyme
D196G/E197A
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complete loss of nitrate reductase activity
E197A
-
mutant enzyme with reduced activity; reduced nitrate reductase activity
M182H
-
complete loss of nitrate reductase activity; inactive mutant enzyme
R421E
-
complete loss of nitrate reductase activity
R421ED196G/E197A
-
inactive mutant enzyme
R421K
-
mutant enzyme with reduced activity; reduced nitrate reductase activity
H49C
P09152
loss of catalytic activity. The midpoint potential value of the [4Fe-4] cluster is decreased by at least 500 mV
R94S
P09152
residue in the vicinity of the [4Fe-4S] cluster. The midpoint potential value of the [4Fe-4] cluster is decreased by 115 mV, with a concomitant decrease in enzyme turnover to 30% of the wild type
H49C
Escherichia coli LCB79
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loss of catalytic activity. The midpoint potential value of the [4Fe-4] cluster is decreased by at least 500 mV
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H49S
Escherichia coli LCB79
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loss of catalytic activity. Both the [4Fe-4S] cluster and the molybdo-bis(pyranopterin guanine dinucleotide) cofactor are absent
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additional information
-
strain FAJ0164: kanamycin-resistant napA insertion mutant expresses assimilatory nitrate reductase, but no NAP and therefore no methyl viologen- or benzyl viologen-dependent nitrate reductase activity
additional information
-
strain FAJ0164: kanamycin-resistant napA insertion mutant expresses assimilatory nitrate reductase, but no NAP and therefore no methyl viologen- or benzyl viologen-dependent nitrate reductase activity
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H49S
P09152
loss of catalytic activity. Both the [4Fe-4S] cluster and the molybdo-bis(pyranopterin guanine dinucleotide) cofactor are absent
additional information
-
deletion of periplasmic enzyme, nitrate-dependent growth is inhibited by sub-mM concentrations of tungstate in the medium
R94S
Escherichia coli LCB79
-
residue in the vicinity of the [4Fe-4S] cluster. The midpoint potential value of the [4Fe-4] cluster is decreased by 115 mV, with a concomitant decrease in enzyme turnover to 30% of the wild type
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additional information
-
strain LP59JG: isogenic mutant deficient in the ability to synthesize the respiratory nitrate reductase, obtained by allelic exchange of a gentamicin resistance gene in the narG gene encoding the catalytic subunit of enzyme
additional information
Pseudomonas fluorescens YT101
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strain LP59JG: isogenic mutant deficient in the ability to synthesize the respiratory nitrate reductase, obtained by allelic exchange of a gentamicin resistance gene in the narG gene encoding the catalytic subunit of enzyme; strain LP59JG: isogenic mutant deficient in the ability to synthesize the respiratory nitrate reductase, obtained by allelic exchange of a gentamicin resistance gene in the narG gene encoding the catalytic subunit of enzyme
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additional information
-
N-terminal his tag, results in hyperbolic kinetics for nitrate
additional information
Synechococcus sp. RF-1
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N-terminal his tag, results in hyperbolic kinetics for nitrate
-
additional information
-
narC::kat mutants without NR activity expresses constitutively NarG and NarJ, but NarG appears in the soluble fraction instead of associated with the membranes
additional information
-
the napA gene is inactivated by inserting a kanamycin resistance gene cassette. The resulting mutant does not grow by nitrate respiration and does not reduce nitrate during growth by fumarate respiration, in contrast to the wild type
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
inoculated of root nodules of Glycine max with Bradyrhizobium japonicum. In the presence of nitrate, all of the nitrosylleg-hemoglobin within normoxic nodules arises from nitrate reduction by the bacterial enzyme, whereas the enzyme is only responsible for half of the nitrosylleg-hemoglobin within hypoxic nodules
medicine
-
potential target for persistence-specific anti-tubercular drug development
synthesis
-
strong correlation of enzyme transcription rate and activity, enzyme activity is highest when growth occurs on butyrate followed by acetate and succinate