Information on EC 1.4.3.8 - ethanolamine oxidase

for references in articles please use BRENDA:EC1.4.3.8
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.4.3.8
-
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RECOMMENDED NAME
GeneOntology No.
ethanolamine oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ethanolamine:oxygen oxidoreductase (deaminating)
A cobamide-protein.
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CAS REGISTRY NUMBER
COMMENTARY hide
9013-00-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
blowfly
-
-
Manually annotated by BRENDA team
Bacterium ATCC 13796, Arthrobacter sp.
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-amino-2-propanol + H2O + O2
2-hydroxy-propionic aldehyde + NH3 + H2O2
show the reaction diagram
3-amino-1-propanol + H2O + O2
3-hydroxy-propionic aldehyde + NH3 + H2O2
show the reaction diagram
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
show the reaction diagram
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanolamine + H2O + O2
glycolaldehyde + NH3 + H2O2
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates the dialyzed enzyme, regeneration of 50% of the initial activity
Ni2+
-
slight stimulation
Zn2+
-
activates the dialyzed enzyme, regeneration of 50% of initial activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
cysteine
Dibenzylamine
-
-
glutathione
hydrazine
hydroxylamine
Iproniazide
-
-
isoniazide
Quinacrine
Semicarbazide
Sodium azide
-
-
Sodium bisulfite
sodium-diethyldithiocarbamate
-
-
additional information
-
not: 8-hydroxyquinoline
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 5
ethanolamine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00026
-
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.2
-
pH 7.0: about 50% of activity maximum, pH 8.2: 37% of activity maximum
7 - 9.8
-
half-maximal activities at pH 7 and pH 9.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26 - 48
-
half-maximal activities at 26°C and 48°C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
-
enzyme more active in larvae than in adults
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity in mitochondria
-
Manually annotated by BRENDA team
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis causes inactivation, activity cannot be restored by addition of pyridoxal phosphate, FAD, NAD+, NADP+ alone or in combination with divalent cations
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-5°C, 6 months, stable
-
more unstable, cannot be stored
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli EG-13 cells
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LINKS TO OTHER DATABASES (specific for EC-Number 1.4.3.8)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)