1.4.3.21: primary-amine oxidase
This is an abbreviated version!
For detailed information about primary-amine oxidase, go to the full flat file.
Word Map on EC 1.4.3.21
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1.4.3.21
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endothelial
-
diamine
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1.4.3.6
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ssaos
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deamination
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polyamines
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leukocyte
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putrescine
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lymphocyte
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spermine
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methylamine
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lysyl
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vessel
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arthrobacter
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extravasation
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phenylhydrazine
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2,4,5-trihydroxyphenylalanine
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globiformis
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elastin
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cadaverine
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klinman
-
biogenic
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aminoguanidine
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half-reaction
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histaminase
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semiquinone
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pargyline
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acrolein
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pyrroloquinoline
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transmigration
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allylamine
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clorgyline
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beta-aminopropionitrile
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aminoacetone
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copper-binding
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self-processing
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quinoproteins
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2-phenylethylamine
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addressins
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deprenyl
-
phenelzine
-
medicine
- 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
Reaction
Synonyms
AGAO, AMAO2, AMAO3, amine oxidase 1, amine oxidase, copper containing, AO1, AO2, AOC2, AOC3, BAO, benzylamine oxidase, bovine plasma amine oxidase, bovine serum amine oxidase, BPAO, BSAO, CAO, Copper amine oxidase, copper amine oxidase 1, copper amine oxidase 8, copper-containing amine oxidase, copper-containing AO, copper-containing monoamine oxidase, copper-dependent amine oxidase, copper/quinone containing amine oxidase, Cu/TPQ amine oxidase, CuAO, CuAO1, CuAO2, CuAO3, CuAO8, EC 1.4.3.6, ECAO, ELAO, GPAO, grass pea amine oxidase, Hansenula polymorpha amine oxidase, HPAO, hPAO-1, HPAO-2, lentil seedling amine oxidase, LSAO, MAO-N, More, OVAO, PAO, pea seedling amine oxidase, plasma amine oxidase, PrAO, primary amine oxidase, primary-amine:oxygen oxidoreductase, PSAO, quinone- and copper-containing amine oxidase, quinone-containing copper amine oxidase, quinone-dependent amine oxidase, quinoprotein copper-containing amine oxidase, RAO, sainfoin amine oxidase, semicarbazide-sensitive amine oxidase, semicarbazide-sensitive amine oxidase/vascular adhesion protein-1, SSAO, SSAO/VAP-1, TPQ-containing CuAO, tynA, tyramine oxidase, copper-requiring, VAP-1, vascular adhesion protein 1, vascular adhesion protein-1
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1.4.3.21 primary-amine oxidaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 1.4.3.21 - primary-amine oxidase
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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
Co2+
Cobalt
-
the Km-value for O2 of the cobalt-substituted enzyme form is approximately 70fold higher than that of the copper-containing wild-type enzyme
copper
Cu
-
only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Cu2+
Ni2+
Zn
-
the presence of substantial amount of zinc results in two distinctive enzyme species, designated as the fast and slow enzymes. Both forms are rapidly reduced by substrate methylamine with a rate constant of 199/s but behave differently in their oxidation rates. The fast enzyme is oxidized by dioxygen at a rate of 22.1/s, whereas the slow enzyme reacts at a rate of 0.00018/s. An investigation of the relationship between the copper content and the extent of the fast enzyme shows that only the copper-containing homodimer is capable of rapid reoxidation and the zinc-copper heterodimers are incapable of rapid turnover at either subunit
Zn2+
additional information
Co2+
enzyme reconstituted with Co2+ exhibits 2.2% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Co2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
copper
-
the purified enzyme contains 2.39 mol of copper per mol of subunit
copper
-
copper depleted enzyme can be reconstituted with either Cu2+, Zn2+, Co2+, or Ni2+, 79% of activity is restored with Cu2+, 19% is restored with Co2+, 1.7% with Zn2+ or Ni2+
copper
-
study of cupric ions by magnetic-resonance and kinetic methods, native enzyme contains 2 tightly bound Cu2+ ions
copper
-
contains 8 Cu2+ per 1200000 Da, Co2+, Zn2+ and Ni2+ can replace Cu2+, no effect of Mn2+
Cu2+
copper protein. The native Cu2+ has essential roles such as catalyzing the electron transfer between the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen, in part by providing a binding site for 1e- and 2e- reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and the aminoresorcinol form of the reduced topaquinone cofactor and dioxygen
Cu2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Cu2+
the wild type enzyme contains 1 mol copper per mol of subunit, copper is the most efficient catalytic metal
Cu2+
the enzyme contains one non-blue copper type 2 ion as an inorganic cofactor
Cu2+
required for activity, the zinc content is 0.4 mol per mole of AOC3 monomer
Cu2+
required for activity, after overnight incubation with 0.1 mM CuSO4, isoform AMAO3 shows slightly enhanced activity (114% of untreated enzyme activity)
Cu2+
required for activity, after overnight incubation with 0.1 mM CuSO4, there is no change in the activity of isoform AMAO2
Ni2+
enzyme reconstituted with Co2+ exhibits 0.9% of the activity of the original Cu2+ -enzyme, KM-values for amine substrate and dioxygen are comparable
Ni2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions can not initiate topaquinone formation under the atmospheric conditions, slow spectral changes are observed in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. X-ray crystallographic analysis reveals structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Co2+ and Ni2+ ions are also capable of forming topaquinone, though much less efficiently than Cu2+
Zn2+
besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ are also bound to the metal site of the apoenzyme so tightly that they are not replaced by excess Cu2+ ions added subsequently
