Probing the Molecular Mechanisms in Copper Amine Oxidases by Generating Heterodimers
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چکیده
منابع مشابه
Probing the Molecular Mechanisms in Copper Amine Oxidases by Generating Heterodimers
For some homodimeric copper amine oxidases (CuAO), there is suggestive evidence of differential activity at the two active sites implying potential cooperativity between the two monomers. To examine this phenomenon for the Arthrobacter globiformis CuAO (AGAO), we purified a heterodimeric form of the enzyme for comparison with the homodimer. The heterodimer comprises an active wild-type monomer ...
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Copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to mol...
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متن کاملInhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine
Copper amine oxidases are important enzymes, which contribute to the regulation of monoand polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to molec...
متن کاملinhibition of chickpea seedling copper amine oxidases by tetraethylenepentamine
copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. each monomer contains one cu(ii) ion and 2,4,5-trihydroxyphenylalanine (tpq) as cofactors. they catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. the mechanism is followed by the transfer of two electrons to mol...
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ژورنال
عنوان ژورنال: ChemBioChem
سال: 2015
ISSN: 1439-4227
DOI: 10.1002/cbic.201402653