Information on EC 1.7.3.6 - hydroxylamine oxidase (cytochrome)

Word Map on EC 1.7.3.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)
Please login to have access to the AMENDA and FRENDA data

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.7.3.6
-
top print hide
RECOMMENDED NAME
GeneOntology No.
hydroxylamine oxidase (cytochrome)
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydroxylamine + 2 ferricytochrome c = nitroxyl + 2 ferrocytochrome c + 2 H+
show the reaction diagram
(1a)
-
-
-
hydroxylamine + O2 = nitrite + H2O + H+
show the reaction diagram
overall reaction
-
-
-
nitroxyl + 2 ferrocytochrome c + O2 + H+ = nitrite + 2 ferricytochrome c + H2O
show the reaction diagram
spontaneous
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
hydroxylamine:oxygen oxidoreductase
The enzyme from the heterotrophic nitrifying bacterium Paracoccus denitrificans contains three to five non-heme, non-iron-sulfur iron atoms and interacts with cytochrome c556 and pseudoazurin [2,3]. Under anaerobic conditions in vitro only nitrous oxide is formed [3]. Presumably nitroxyl is released and combines with a second nitroxyl to give nitrous oxide and water. When oxygen is present, nitrite is formed.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9075-43-8
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxylamine + ferricytochrome c550
nitroxyl + ferrocytochrome c550 + H+
show the reaction diagram
-
under aerobic assay conditions nitrite is the major reaction product but N2O is also detected at low levels. Under anaerobic conditions no nitrite is produced but N2O is detected, though at non-stoichiometric levels. The production of nitrite by Paracoccus denitrificans hydroxylamine oxidase is an oxygen-dependent reaction
-
-
?
hydroxylamine + ferricytochrome c551
nitroxyl + ferrocytochrome c551 + H+
show the reaction diagram
-
-
-
-
?
hydroxylamine + horse heart ferricytochrome c
nitroxyl + horse heart ferrocytochrome c + H+
show the reaction diagram
hydroxylamine + O2
nitrite + H2O + H+
show the reaction diagram
hydroxylamine + pseudoazurin
nitrite + reduced pseudoazurin
show the reaction diagram
additional information
?
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
non-heme iron enzyme, the enzyme could possess a non-heme ferric iron centre that is lost when the 20000 Da polypeptide is subjected to SDS-PAGE, but that can be reconstituted by addition of Fe3+ ions to the refolded enzyme
Fe2+
-
the enzyme is activated 6fold and 21fold by 0.01 mM and 0.1 mM ferrous ions, respectively
Iron
-
contains 3-5 nonhaem, non-iron-sulfur iron atoms as prosthetic groups, predominantly coordinated by carboxylate ligands
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
-
the cyanide-sensitive form of the enzyme exists only during turnover
H2O2
-
irreversible, inactivation most rapid at pH 9-10, overview: substrates which protect against inactivation
NaCl
-
15 mM, 50% inhibition of activity with horse heart cytochrome, activity with pseudoazurin or cytochrome c550 is inhibited only above 100 mM
additional information
-
hardly inhibited by 0.1 mM KCN
-
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
ferricytochrome c551
-
pH 7.8, 25°C
-
0.07
horse heart ferricytochrome c
-
in 10 mM Tris-HC1 (pH 8.0), at 30°C
-
0.35
hydroxylamine
-
in 10 mM Tris-HC1 (pH 8.0), at 30°C
0.033
pseudoazurin
-
pH 7.8, 25°C
-
top print hide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
hydroxylamine
Paracoccus denitrificans
-
pH 8, temperature not specified in the publication
top print hide
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
EDTA
Arthrobacter globiformis
-
at pH 9.0 and 30°C
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
-
in 10 mM Tris-HC1 (pH 8.0), at 30°C
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
activity with horse heart cytochrome c
10
-
activity with pseudoazurin
11
-
activity with cytochrome c550 continues to increase to pH 11
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 11.5
-
pH 7.3: about 35% of maximal activity, pH 11.5: about 50% of maximal activity activity with pseudoazurin
7.6 - 10
-
pH 7.6: about 50% of maximal activity, pH 10.0: about 35% of maximal activity with horse heart cytochrome c
8 - 11
-
activity with cytochrome c550 continues to increase to pH 11, activity at pH 8 is about 50% of the activity at pH 11
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
-
x * 19000, SDS-PAGE
20000
-
x * 20000, SDS-PAGE
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
90% loss of activity after 1 min at 70°C
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in energy-depleted cells, hao 3 gene expression is increased in the presence of 30 mM NH4+
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.7.3.6)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)