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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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).
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
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
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
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
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
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
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
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
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
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
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
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
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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