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Information on EC 1.4.3.21 - primary-amine oxidase and Organism(s) Pisum sativum and UniProt Accession Q43077
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1.4.3.21 primary-amine oxidaseIUBMB Comments
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
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Word Map
- 1.4.3.21
- endothelial
- diamine
-
1.4.3.6
-
ssaos
-
deamination
- polyamines
- leukocyte
- putrescine
- lymphocyte
- spermine
- methylamine
-
lysyl
- vessel
- arthrobacter
-
extravasation
- phenylhydrazine
-
2,4,5-trihydroxyphenylalanine
- globiformis
- elastin
- cadaverine
-
klinman
-
biogenic
- aminoguanidine
-
half-reaction
- histaminase
- semiquinone
- pargyline
- acrolein
-
pyrroloquinoline
-
transmigration
- allylamine
- clorgyline
- beta-aminopropionitrile
- aminoacetone
-
copper-binding
-
self-processing
-
quinoproteins
- 2-phenylethylamine
-
addressins
- deprenyl
- phenelzine
- medicine
The taxonomic range for the selected organisms is: Pisum sativum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
vap-1, vascular adhesion protein-1, copper amine oxidase, benzylamine oxidase, bovine serum amine oxidase, plasma amine oxidase, ssao/vap-1, bovine plasma amine oxidase, copper-containing amine oxidase, primary amine oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
primary-amine:oxygen oxidoreductase (deaminating)
A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
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
4-aminomethylpyridine dihydrochloride + H2O + O2
?
less than 0.1% substrate activity of 1 mM 4-aminomethylpyridine dihydrochloride as percentage of the activity of the best substrate (putrescine, 1 mM) for various amine oxidases
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-diamino-2-butyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,4-diamino-2-chloro-2-butene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,5-diamino-2-pentyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
1,6-diamino-2,4-hexadiyne
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
2-Bromoethylamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3,3-bis(aminoethyl)-1-hydroxy-2-oxo-1-triazene
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
N6-(4-aminobut-2-ynyl)adenine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tryptamine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
tyramine
during the oxidation of these suicide substrates, the reversible formation of an enzyme-killer product complex occurs followed by an irreversible inactivation of the enzyme, typical of mechanism-based inactivation
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.026
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
1
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.29
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.57
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.1
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
99
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
152
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
82
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
160
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.1
O2
-
cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
3320
O2
-
wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
4640
O2
-
copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
270
putrescine
-
wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
280
putrescine
-
copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
3-cycloheptylamino-4-aminomethylpyridine dihydrochloride monohydrate
Pisum sativum
-
0.89
3-cyclohexylmethylamino-4-aminomethylpyridine dihydrochloride monohydrate
Pisum sativum
-
0.055
4-(aminomethyl)-N,N'-diethylpyridine-3,5-diamine dihydrochloride
Pisum sativum
-
0.017
4-(aminomethyl)-N,N'-dimethylpyridine-3,5-diamine dihydrochloride
Pisum sativum
-
additional information
additional information
Pisum sativum
above 0.1 mM for 2-methylaminobenzylamine dihydrochloride and 2-ethylaminobenzylamine dihydrochloride
-
additional information
additional information
Pisum sativum
-
above 0.1 mM for 2-methylaminobenzylamine dihydrochloride and 2-ethylaminobenzylamine dihydrochloride
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.016
-
copper-depleted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
0.38
-
cobalt-substituted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
13.6
-
wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
7
-
copper-reconstituted wild type enzyme, with 4-N,N-dimethylaminomethyl benzylamine as substrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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). AMO_PEA
674
1
76358
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
topaquinone is derived by post-translational modification of a conserved tyrosine residue in the protein chain
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63
when incubated at 63 °C the enzyme loses more than 90% of its activity in the first hour while in presence of 1 M sucrose, its inactivation appears after 10 min incubation at 70°C
70
when incubated at 63 °C the enzyme loses more than 90% of its activity in the first hour while in presence of 1 M sucrose, its inactivation appears after 10 min incubation at 70°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sucrose stabilizes the enzyme in terms of activity, secondary and tertiary structure. On the other hand sucrose reduces unfolding rate constant at given temperature. These effects can be the result of strengthening the water cage around the protein which limits oscillation frequency of the protein during unfolding process
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bertini, V.; Buffoni, F.; Ignesti, G.; Picci, N.; Trombino, S.; Iemma, F.; Alfei, S.; Pocci, M.; Lucchesini, F.; De Munno, A.
Alkylamino derivatives of 4-aminomethylpyridine as inhibitors of copper-containing amine oxidases
J. Med. Chem.
48
664-670
2005
Sus scrofa, Ogataea angusta (P12807), Ogataea angusta, Pisum sativum (Q42432), Pisum sativum
Longu, S.; Mura, A.; Padiglia, A.; Medda, R.; Floris, G.
Mechanism-based inactivators of plant copper/quinone containing amine oxidases
Phytochemistry
66
1751-1758
2005
Lens culinaris, Onobrychis viciifolia, Pisum sativum (Q43077), Lathyrus sativus (Q6A174)
Mills, S.A.; Brown, D.E.; Dang, K.; Sommer, D.; Bitsimis, A.; Nguyen, J.; Dooley, D.M.
Cobalt substitution supports an inner-sphere electron transfer mechanism for oxygen reduction in pea seedling amine oxidase
J. Biol. Inorg. Chem.
17
507-515
2012
Pisum sativum
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