Ethanolamine oxidase from the blowfly, Phormia regina (Diptera: Insecta)
Kulkarni, A.P.; Hodgson, E.; Comp. Biochem. Physiol. B 44, 407-422 (1973) 
Data extracted from this reference:
Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
no stimulation of activity by FAD, pyridoxalphosphate, NAD+, NADP+
Phormia regina
General Stability
General Stability
Organism
dialysis causes inactivation, activity cannot be restored by addition of pyridoxal phosphate, FAD, NAD+, NADP+ alone or in combination with divalent cations
Phormia regina
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Phormia regina
Co2+
-
Phormia regina
cysteine
-
Phormia regina
Dibenzylamine
-
Phormia regina
glutathione
no effect
Phormia regina
hydrazine
-
Phormia regina
hydroxylamine
-
Phormia regina
KCN
-
Phormia regina
additional information
not: 8-hydroxyquinoline
Phormia regina
Quinacrine
-
Phormia regina
Semicarbazide
-
Phormia regina
Sodium azide
-
Phormia regina
Sodium bisulfite
-
Phormia regina
sodium-diethyldithiocarbamate
-
Phormia regina
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.16
-
ethanolamine
-
Phormia regina
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Phormia regina
5737
-
additional information
no activity in mitochondria
Phormia regina
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates the dialyzed enzyme, regeneration of 50% of the initial activity
Phormia regina
Ni2+
slight stimulation
Phormia regina
Zn2+
activates the dialyzed enzyme, regeneration of 50% of initial activity
Phormia regina
Organism
Organism
UniProt
Commentary
Textmining
Phormia regina
-
blowfly
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Phormia regina
Source Tissue
Source Tissue
Commentary
Organism
Textmining
egg
low activity
Phormia regina
-
larva
-
Phormia regina
-
pupa
low activity
Phormia regina
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00026
-
-
Phormia regina
Storage Stability
Storage Stability
Organism
more unstable, cannot be stored
Phormia regina
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ethanolamine + H2O + O2
under aerobic conditions
391967
Phormia regina
glycolaldehyde + NH3 + H2O2
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Phormia regina
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
26
48
half-maximal activities at 26°C and 48°C
Phormia regina
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Phormia regina
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
8.2
pH 7.0: about 50% of activity maximum, pH 8.2: 37% of activity maximum
Phormia regina
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
no stimulation of activity by FAD, pyridoxalphosphate, NAD+, NADP+
Phormia regina
General Stability (protein specific)
General Stability
Organism
dialysis causes inactivation, activity cannot be restored by addition of pyridoxal phosphate, FAD, NAD+, NADP+ alone or in combination with divalent cations
Phormia regina
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
-
Phormia regina
Co2+
-
Phormia regina
cysteine
-
Phormia regina
Dibenzylamine
-
Phormia regina
glutathione
no effect
Phormia regina
hydrazine
-
Phormia regina
hydroxylamine
-
Phormia regina
KCN
-
Phormia regina
additional information
not: 8-hydroxyquinoline
Phormia regina
Quinacrine
-
Phormia regina
Semicarbazide
-
Phormia regina
Sodium azide
-
Phormia regina
Sodium bisulfite
-
Phormia regina
sodium-diethyldithiocarbamate
-
Phormia regina
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.16
-
ethanolamine
-
Phormia regina
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytoplasm
-
Phormia regina
5737
-
additional information
no activity in mitochondria
Phormia regina
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates the dialyzed enzyme, regeneration of 50% of the initial activity
Phormia regina
Ni2+
slight stimulation
Phormia regina
Zn2+
activates the dialyzed enzyme, regeneration of 50% of initial activity
Phormia regina
Purification (Commentary) (protein specific)
Commentary
Organism
-
Phormia regina
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
egg
low activity
Phormia regina
-
larva
-
Phormia regina
-
pupa
low activity
Phormia regina
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.00026
-
-
Phormia regina
Storage Stability (protein specific)
Storage Stability
Organism
more unstable, cannot be stored
Phormia regina
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ethanolamine + H2O + O2
under aerobic conditions
391967
Phormia regina
glycolaldehyde + NH3 + H2O2
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Phormia regina
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
26
48
half-maximal activities at 26°C and 48°C
Phormia regina
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Phormia regina
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
8.2
pH 7.0: about 50% of activity maximum, pH 8.2: 37% of activity maximum
Phormia regina
Other publictions for EC 1.4.3.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742141
Pereira
Engineering a novel biosynthe ...
Arthrobacter sp. FERM P-06240
Biotechnol. Bioeng.
113
376-383
2016
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1
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1
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391967
Kulkarni
Ethanolamine oxidase from the ...
Phormia regina
Comp. Biochem. Physiol. B
44
407-422
1973
1
-
-
-
-
1
14
1
2
3
-
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3
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1
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3
1
1
1
-
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1
1
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-
1
1
-
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1
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1
-
14
-
1
2
3
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-
1
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3
1
1
1
-
1
1
-
-
1
1
-
-
-
-
-
-
-
-
391965
Narrod
-
Ethanolamine oxidase ...
Pseudomonas sp.
Methods Enzymol.
8
354-357
1966
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10
1
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1
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1
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1
1
4
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1
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10
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1
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1
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1
1
4
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1
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391966
Narrod
Metabolism of ethanolamine, an ...
Pseudomonas sp.
J. Biol. Chem.
239
2189-2193
1964
1
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10
1
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1
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1
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1
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1
1
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5
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1
1
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1
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10
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1
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1
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1
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1
1
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5
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1
1
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