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Information on EC 1.4.3.21 - primary-amine oxidase and Organism(s) Escherichia coli, Escherichia coli K-12
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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: Escherichia coli
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
additional information
?
-
the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699
-
-
?
additional information
?
-
-
the catalytic reaction proceeds via two half-reactions; the aldehyde product is released at the end of the reductive half-reaction before reduction of molecular oxygen in the oxidative half-reaction. Mechanism of molecular oxygen entry into the buried active site of the copper amine oxidase, the N-terminal domain does not affect oxygen entry, overview. The protein-derived cofactor TPQ and the off-metal O2-binding site are located in the vicinity of a conserved active-site Met699
-
-
?
additional information
?
-
-
the enzyme can use human granulocytes as a substrate
-
-
?
NATURAL SUBSTRATE
NATURAL 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
calcium is the normal ligand of these peripheral sites. Enzyme activity is stimulated by 3 mM. Removal of the not solvent exposed calcium ion with EDTA results in a 60-90% reduction in enzyme activity
Cu2+
additional information
Cu2+
the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
2-Phenylethylamine
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.4
2-Phenylethylamine
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10330
2-Phenylethylamine
wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Escherichia coli copper amine oxidase possesses an extra N-terminal domain that lies close to one entrance to the beta-sandwich in the structurally conserved beta-sandwich structure
additional information
-
Escherichia coli copper amine oxidase possesses an extra N-terminal domain that lies close to one entrance to the beta-sandwich in the structurally conserved beta-sandwich structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme with xenon is used as a molecular oxygen binding-site probe, 8 mg/ml protein in 100 mM HEPES pH 7 and 1.2 M sodium citrate, vappour diffusion method, 18°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D383E
-
turnover-number of mutant enzyme is reduced up to 2000fold, depending on pH-value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saysell, C.G.; Tambyrajah, W.S.; Murray, J.M.; Phillips, S.V.; McPherson, M.J.; Knowles, P.F.
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue
Biochem. J.
365
809-816
2002
Escherichia coli
Pirrat, P.; Smith, M.A.; Pearson, A.R.; McPherson, M.J.; Phillips, S.E.
Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway
Acta Crystallogr. Sect. F
64
1105-1109
2008
Escherichia coli (P46883), Escherichia coli
Smith, M.A.; Pirrat, P.; Pearson, A.R.; Kurtis, C.R.; Trinh, C.H.; Gaule, T.G.; Knowles, P.F.; Phillips, S.E.; McPherson, M.J.
Exploring the roles of the metal ions in Escherichia coli copper amine oxidase
Biochemistry
49
1268-1280
2010
Escherichia coli (P46883), Escherichia coli
Elovaara, H.; Huusko, T.; Maksimow, M.; Elima, K.; Yegutkin, G.G.; Skurnik, M.; Dobrindt, U.; Siitonen, A.; McPherson, M.J.; Salmi, M.; Jalkanen, S.
Primary amine oxidase of Escherichia coli is a metabolic enzyme that can use a human leukocyte molecule as a substrate
PLoS ONE
10
e0142367
2015
Escherichia coli
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