Inner-Sphere Mechanism for Molecular Oxygen Reduction Catalyzed by Copper Amine Oxidases
نویسندگان
چکیده
منابع مشابه
Inhibition 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...
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 کاملCompetitive inhibition of copper amine oxidases by vitamin B hydrochloride in chickpea
Copper amine oxidases (CAOs) catalyse the oxidative de-amination of biogenic amines which are ubiquitous compounds essential for cell growth and proliferation. The enzymes are homodimers containing both topaquinone and a Cu(II) ions as cofactors at the active site of each subunit. After extraction and purification of chickpea (cicer arietinum) amine oxidase by chromatoghraphy, Km and Vmax of th...
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...
متن کاملProbing 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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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2008
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja801378f