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Information on EC 1.7.2.5 - nitric oxide reductase (cytochrome c) and Organism(s) Fusarium oxysporum and UniProt Accession P23295

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IUBMB Comments
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre comprising a non-heme iron centre and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551
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This record set is specific for:
Fusarium oxysporum
UNIPROT: P23295
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The taxonomic range for the selected organisms is: Fusarium oxysporum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nitric oxide reductase, no reductase, p450nor, flavorubredoxin, norcb, nitric-oxide reductase, norbc, no-reductase, ba3-oxidase, nitric oxide reductase cytochrome, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitric oxide reductase cytochrome
-
nitric oxide reductase
-
-
nitrogen oxide reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nitrous oxide:ferricytochrome-c oxidoreductase
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre comprising a non-heme iron centre and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551
CAS REGISTRY NUMBER
COMMENTARY hide
37256-43-2
-
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 + NADH + H+
nitrous oxide + NAD+
show the reaction diagram
cytochrome P450nor is a nitric oxide reductase involved in fungal denitrification
-
-
?
2 nitric oxide + reduced acceptor
nitrous oxide + acceptor + H2O
show the reaction diagram
nitric oxide + NADH
nitrous oxide + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
NO + NADH
N2O + H2O + 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 + NADH + H+
nitrous oxide + NAD+
show the reaction diagram
cytochrome P450nor is a nitric oxide reductase involved in fungal denitrification
-
-
?
2 nitric oxide + reduced acceptor
nitrous oxide + acceptor + H2O
show the reaction diagram
-
-
-
-
?
NO + NADH
N2O + H2O + NAD+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
the tautomer Fe(III)-ON(OH2)(NO) is the catalytically productive species that spontaneously cleaves the N-OH2 bond forming N2O and H2O in a highly exergonic reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
NADH
-
-
0.06
NO
-
NADH as electron acceptor
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
211 - 525
NO
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NOR_FUSOX
403
0
44372
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
-
1 * 46000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 46000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at cryogenic temperature -173°C wild-type, S286V- and S286T-mutant
-
in the ferric resting and in the ferrous carbonmonoxy states, at 1.0 and 1.05 A resolution, respectively
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sitting drop vapour diffusion, crystals diffract to less than 2.0 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A239K
-
6% activity of modified soluble wild-type enzyme
A242K
-
42% activity of modified soluble wild-type enzyme
G240K
-
63% activity of modified soluble wild-type enzyme
M244K
-
60% activity of modified soluble wild-type enzyme
M247K
-
130% activity of modified soluble wild-type enzyme
N241K
-
38% activity of modified soluble wild-type enzyme
N246K
-
45% activity of modified soluble wild-type enzyme
S286T
-
7% activity of wild-type
S286V
-
1% activity of wild-type
T243H
-
8% activity of modified soluble wild-type enzyme
T243K
-
12% activity of modified soluble wild-type enzyme
T243R
-
17% activity of modified soluble wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in the soluble fraction of Escherichia coli JM109, modified N-terminus, 92% activity of wild-type
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shimizu, H.; Park, S.Y.; Shiro, Y.; Adachi, S.
X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution
Acta Crystallogr. Sect. D
58
81-89
2002
Fusarium oxysporum
Manually annotated by BRENDA team
Hendriks, J.; Oubrie, A.; Castresana, J.; Urbani, A.; Gemeinhardt, S.; Saraste, M.
Nitric oxide reductases in bacteria
Biochim. Biophys. Acta
1459
266-273
2000
Cupriavidus necator, Alcaligenes faecalis, Geobacillus stearothermophilus, Bradyrhizobium japonicum, Corynebacterium diphtheriae, Fungi, Fusarium oxysporum, Paracoccus denitrificans, Halomonas halodenitrificans, Staphylococcus aureus, Mycobacterium avium, Neisseria gonorrhoeae, Neisseria meningitidis, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas stutzeri, Cereibacter sphaeroides
Manually annotated by BRENDA team
Shimizu, H.; Obayashi, E.; Gomi, Y.; Arakawa, H.; Park, S.Y.; Nakamura, H.; Adachi, S.I.; Shoun, H.; Shiro, Y.
Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes
J. Biol. Chem.
275
4816-4826
2000
Fusarium oxysporum
Manually annotated by BRENDA team
Singh, U.P.; Obayashi, E.; Takahashi, S.; Iizuka, T.; Shoun, H.; Shiro, Y.
The effects of heme modification on reactivity, ligand binding properties and iron-coordination structures of cytochrome P450nor
Biochim. Biophys. Acta
1384
103-111
1998
Fusarium oxysporum
Manually annotated by BRENDA team
Okamoto, N.; Tsuruta, K.; Imai, Y.; Tomura, D.; Shoun, H.
Fungal P450nor: expression in Escherichia coli and site-directed mutagenesis at the putative distal region
Arch. Biochem. Biophys.
337
338-344
1997
Fusarium oxysporum
Manually annotated by BRENDA team
Toritsuka, N.; Shoun, H.; Singh, U.P.; Park, S.Y.; Iizuka, T.; Shiro, Y.
Functional and structural comparison of nitric oxide reductases from denitrifying fungi Cylindrocarpon tonkinense and Fusarium oxysporum
Biochim. Biophys. Acta
1338
93-99
1997
Fusarium lichenicola, Fusarium oxysporum
Manually annotated by BRENDA team
Daiber, A.; Shoun, H.; Ullrich, V.
Nitric oxide reductase (P450nor) from Fusarium oxysporum
J. Inorg. Biochem.
99
185-193
2005
Fusarium oxysporum
Manually annotated by BRENDA team
Lehnert, N.; Praneeth, V.K.; Paulat, F.
Electronic structure of iron(II)-porphyrin nitroxyl complexes: molecular mechanism of fungal nitric oxide reductase (P450nor)
J. Comput. Chem.
27
1338-1351
2006
Fusarium oxysporum
Manually annotated by BRENDA team
Zhang, L.; Shoun, H.
Purification and functional analysis of fungal nitric oxide reductase cytochrome P450nor
Methods Enzymol.
437
117-133
2008
Fusarium oxysporum (P23295), Fusarium lichenicola (Q00616), Fusarium lichenicola (Q12599), Aspergillus oryzae (Q8NKB4), Cutaneotrichosporon cutaneum (Q96WS9)
Manually annotated by BRENDA team