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Information on EC 1.14.12.17 - nitric oxide dioxygenase and Organism(s) Cupriavidus necator and UniProt Accession P39662

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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:
Cupriavidus necator
UNIPROT: P39662
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Word Map
The taxonomic range for the selected organisms is: Cupriavidus necator
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cytoglobin, vitreoscilla hemoglobin, flavohemoglobin, no dioxygenase, nitric oxide dioxygenase, flavohb, hemoglobin n, barley hemoglobin, nitric-oxide dioxygenase, no degrading dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavohemoglobin
-
nitric oxide dioxygenase
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flavohemoglobin
-
flavoHb
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 + NAD(P)H
NO3- + NAD(P)+ + H+
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbon monoxide
competitive inhibition
clotrimazole
-
-
econazole
-
-
ketoconazol
-
-
miconazole
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
O2
apparent KM
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
carbon monoxide
Ki value less than 1 microM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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