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Information on EC 1.14.12.17 - nitric oxide dioxygenase and Organism(s) Escherichia coli and UniProt Accession P24232

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IUBMB Comments
A flavohemoglobin (FAD). It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
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This record set is specific for:
Escherichia coli
UNIPROT: P24232
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cytoglobin, vitreoscilla hemoglobin, flavohemoglobin, no dioxygenase, flavohb, nitric oxide dioxygenase, hemoglobin n, barley hemoglobin, nitric-oxide dioxygenase, no degrading dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavohemoglobin
-
nitric oxide dioxygenase
-
flavoHb
-
-
flavohemoglobin
nitric oxide dioxygenase
-
the chemistry of a synthetic oxy-heme is reported, which exhibits NOD reactivity, where the intermediacy of a peroxynitrite species is implicated
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
SYSTEMATIC NAME
IUBMB Comments
nitric oxide,NAD(P)H:oxygen oxidoreductase
A flavohemoglobin (FAD). It has been proposed that FAD functions as the electron carrier from NADPH to the ferric heme prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY hide
214466-78-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nitric oxide + O2 + NAD(P)H
nitrate + NAD(P)+ + H+
show the reaction diagram
-
-
-
?
NO + O2 + e-
NO3-
show the reaction diagram
-
-
-
-
?
NO + O2 + NAD(P)H
NO3- + NAD(P)+ + H+
show the reaction diagram
-
-
-
-
?
NO + O2 + NADH
NO3- + NAD+
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nitric oxide + O2 + NAD(P)H
nitrate + NAD(P)+ + H+
show the reaction diagram
-
-
-
?
NO + O2 + e-
NO3-
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbon monoxide
competitive inhibition
clotrimazole
-
-
econazole
-
-
imidazole
-
imidazoles coordinate the heme iron atom, impair ferric heme reduction, produce uncompetitive inhibition with respect to O2 and NO and inhibit NO metabolism
ketoconazol
-
-
ketoconazole
-
-
miconazole
NO
-
high concentrations, competition with O2, augmented by miconazole
Superoxide dismutase
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hemin
-
maximal activity at 0.001 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
O2
apparent KM
0.0032 - 0.0048
NADH
0.18
NADPH
-
at 20°C
0.00011 - 0.00028
NO
0.013 - 0.1
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50 - 83
NADH
94 - 670
NO
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
clotrimazole
-
-
0.00055
econazole
-
-
0.005
ketoconazole
-
-
0.00008
miconazole
-
-
additional information
carbon monoxide
Ki value less than 1 microM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0058
-
strain DH5alpha
0.015
-
strain AB1157
0.2095
-
strain DH5alpha after NO-exposition
0.865
-
mutant strain PG118
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
heterologous expression within a lentiviral delivery system results in markedly increased NADPH consumption, which is dependent on the addition of exogenous NO. Expression does not exhibit any noticeable toxicity or growth suppression in several tested mammalian cell types. Flavohemoglobin metabolizes endogenously synthesized NO to NO3- in mammalian cells without affecting NO synthesis itself
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilizing of activity during gel filtration by adding 10 mM NaN3
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous expression within a lentiviral delivery system
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
heterologous expression of Escherichia coli flavohemoglobin within a lentiviral delivery system boosts endogenous cellular consumption of NO, thus providing a simple and efficacious approach to studying mammalian NO-biology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gardner, P.R.; Gardner, A.M.; Martin, L.A.; Salzman, A.L.
Nitric oxide dioxygenase: an enzymic function for flavohemoglobin
Proc. Natl. Acad. Sci. USA
95
10378-10383
1998
Escherichia coli
Manually annotated by BRENDA team
Gardner, P.R.; Costantino, G.; Salzman, A.L.
Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase
J. Biol. Chem.
273
26528-26533
1998
Escherichia coli
Manually annotated by BRENDA team
Gardner, A.M.; Martin, L.A.; Gardner, P.R.; Dou, Y.; Olson, J.S.
Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
J. Biol. Chem.
275
12581-12589
2000
Escherichia coli
Manually annotated by BRENDA team
Helmick, R.A.; Fletcher, A.E.; Gardner, A.M.; Gessner, C.R.; Hvitved, A.N.; Gustin, M.C.; Gardner, P.R.
Imidazole antibiotics inhibit the nitric oxide dioxygenase function of microbial flavohemoglobin
Antimicrob. Agents Chemother.
49
1837-1843
2005
Saccharomyces cerevisiae, Candida albicans, Escherichia coli
Manually annotated by BRENDA team
Gardner, P.R.; Gardner, A.M.; Brashear, W.T.; Suzuki, T.; Hvitved, A.N.; Setchell, K.D.; Olson, J.S.
Hemoglobins dioxygenate nitric oxide with high fidelity
J. Inorg. Biochem.
100
542-550
2006
Escherichia coli
Manually annotated by BRENDA team
Gardner, P.R.
Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
J. Inorg. Biochem.
99
247-266
2005
Cupriavidus necator, Bacillus subtilis, Saccharomyces cerevisiae, Deinococcus radiodurans, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Mowat, C.G.; Gazur, B.; Campbell, L.P.; Chapman, S.K.
Flavin-containing heme enzymes
Arch. Biochem. Biophys.
493
37-52
2010
Saccharomyces cerevisiae, Escherichia coli (P24232), Cupriavidus necator (P39662)
Manually annotated by BRENDA team
Schopfer, M.P.; Mondal, B.; Lee, D.H.; Sarjeant, A.A.; Karlin, K.D.
Heme/O2/*NO nitric oxide dioxygenase (NOD) reactivity: phenolic nitration via a putative heme-peroxynitrite intermediate
J. Am. Chem. Soc.
131
11304-11305
2009
Escherichia coli, Mammalia
Manually annotated by BRENDA team
Forrester, M.T.; Eyler, C.E.; Rich, J.N.
Bacterial flavohemoglobin: a molecular tool to probe mammalian nitric oxide biology
Biotechniques
50
41-45
2011
Escherichia coli
Manually annotated by BRENDA team