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Information on EC 1.4.3.4 - monoamine oxidase and Organism(s) Sus scrofa and UniProt Accession Q6Q2J0
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1.4.3.4 monoamine oxidaseIUBMB Comments
A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines . Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide.
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- 1.4.3.4
- dopamine
-
antidepressant
- parkinsonism
- platelet
-
dopaminergic
-
neurotransmitter
-
tricyclic
- norepinephrine
- pargyline
-
reuptake
- deprenyl
-
deamination
- clorgyline
- catecholamine
- noradrenaline
- 5-hydroxytryptamine
-
neuroprotective
-
serotonergic
- striatal
-
anxiety
-
psychiatric
- l-dopa
- fluoxetine
- catechol-o-methyltransferase
- 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
biogenic
- levodopa
-
mood
- reserpine
- imipramine
-
monoaminergic
- tryptamine
-
3,4-dihydroxyphenylacetic
- benzodiazepine
- mpp+
- amphetamine
-
nigrostriatal
-
homovanillic
-
5-hydroxyindoleacetic
-
noradrenergic
-
dopac
- 5-hydroxytryptophan
- 1-methyl-4-phenylpyridinium
- paroxetine
- desipramine
-
electroconvulsive
-
panic
-
mptp-induced
-
anticholinergic
-
antidepressant-like
- drug development
- analysis
- synthesis
- medicine
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
monoamine oxidase, mao-b, mao-a, monoamine oxidase a, mao a, mao b, monoamine oxidase b, monoamine oxidase-b, monoamine oxidase-a, semicarbazide-sensitive amine oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adrenaline oxidase
-
-
-
-
epinephrine oxidase
-
-
-
-
MAO
-
-
-
-
monoamine oxidase
-
-
-
-
monoamine:O2 oxidoreductase (deaminating)
-
-
-
-
serotonin deaminase
-
-
-
-
tyraminase
-
-
-
-
tyramine oxidase
-
-
-
-
additional information
additional information
-
MAO-A and MAO-B are 2 different isoenzymic forms which differ in substrate specificity, distribution among tissues and their structures
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
amine:oxygen oxidoreductase (deaminating)
A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide.
CAS REGISTRY NUMBER
COMMENTARY
9001-66-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-methylbenzylamine + H2O + O2
alpha-methylbenzaldehyde + NH3 + H2O2
-
-
-
-
r
serotonin + H2O + O2
(5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
serotonin + H2O + O2
(5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km of membrane-bound and Triton X-100-solubilized enzyme
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AOFA_PIG
527
1
59763
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
-
gel filtration, lowest molecular weight determined, variations due to different states of aggregation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme is bound to the mitochondria by acidic phospholipids, soluble enzyme can form complexes with such phospholipids
additional information
-
lipid environment is essential for enzymatic activity, lipid microenvironment may regulate the mode of action of the enzyme in the mitochondrial outer membrane
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
when enzyme liberated by methyl ethyl ketone extraction Km about 3times lower than that for enzyme bound to the mitochondria or solubilzed by Triton X-100
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
both (R)-(-)- and (S)-(+)-1-(1-[11C]methyl-1H-pyrrol-2-yl)-2-phenyl-2-(1-pyrrolidinyl)ethanone are very promising tracers for positron emission tomography of the MAO-A enzyme in brain. The carbon-11-labeling reaction is fairly simple and robust. Yields of more than 1 GBq are routinely obtained and with high specific activity of the final product. The metabolism of (R)-(-)- and (S)-(+)-1-(1-[11C]methyl-1H-pyrrol-2-yl)-2-phenyl-2-(1-pyrrolidinyl)ethanone is relatively slow in plasma of living pigs, in contrast to [11C]harmine, which is difficult to detect in plasma at times after 10 min. Parametric maps of [11C](R)-(-)- and (S)-(+)-1-(1-[11C]methyl-1H-pyrrol-2-yl)-2-phenyl-2-(1-pyrrolidinyl)ethanone binding are qualitatively very comparable to those of [11C]harmine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tipton, K.F.
The prosthetic groups of pig brain mitochondrial monoamine oxidase
Biochim. Biophys. Acta
159
451-459
1968
Sus scrofa
Oreland, L.
Purification and properties of pig liver mitochondrial monoamine oxidase
Arch. Biochem. Biophys.
146
410-412
1971
Sus scrofa
Tipton, K.F.; Spires, I.P.C.
The kinetics of phenethylhydrazine oxidation by monoamine oxidase
Biochem. J.
125
521-524
1971
Rattus norvegicus, Sus scrofa
Inagaki, T.; Rao, N.A.; Yagi, K.
Modulation by phospholipids of the activity of monoamine oxidase purified from pig liver
J. Biochem.
100
597-603
1986
Sus scrofa
Lindstrm, A.; Olsson, B.; Petterson, G.; Szymanska, J.
Kinetics of the interaction between pig-plasma benzylamine oxidase and various monoamines
Eur. J. Biochem.
47
99-105
1974
Sus scrofa
Jensen, S.B.; Di Santo, R.; Olsen, A.K.; Pedersen, K.; Costi, R.; Cirilli, R.; Cumming, P.
Synthesis and cerebral uptake of 1-(1-[(11)C]methyl-1H-pyrrol-2-yl)-2-phenyl-2-(1-pyrrolidinyl)ethanone, a novel tracer for positron emission tomography studies of monoamine oxidase type A
J. Med. Chem.
51
1617-1622
2008
Sus scrofa (Q6Q2J0), Sus scrofa
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