Oxygen activation in a copper-containing amine oxidase
Biochemical Society Transactions, 2003The process by which molecular oxygen is activated to enable it to function as an electron acceptor in biology is poorly understood. The quinoprotein copper-containing amine oxidase (CuAO) catalyses the conversion of primary amines into aldehydes. As well as copper, the enzyme contains an organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ ...
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Biochemical aspects and functional role of the copper-containing amine oxidases
InflammoPharmacology, 2003The copper-containing amine oxidases of the class EC 1.4.3.6 share many biochemical similarities. They contain cupric copper and catalyse the same general reaction. In mammals, diamine oxidase has a role in the metabolism of histamine, some other diamines and spermine oxidase, involved in the metabolism of polyamines.
F, Buffoni, G, Ignesti
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Variable temperature magnetic circular dichroism spectroscopy of copper-containing amine oxidases.
Petra N. Turowski +2 more
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Copper-Containing Amine Oxidases
1989Amine oxidases catalyze the reaction $$ R - C{H_2}NH_3^{+} \quad + \quad {O_2}\quad + \quad {H_2}O \to R - CHO\quad + \quad NH_4^{+} \quad + \quad {H_2}{O_2} $$ where R can be either aromatic or aliphatic. The copper-containing amine oxidases (Cu-AOs) oxidize only primary amines at variance with FAD-containing amine oxidases (eg.
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Structure and Reactivity of Copper-Containing Amine Oxidases
1993In recent years, considerable progress has been made toward understanding the active site structures and mechanisms of copper-containing amine oxidases. Copper-containing amine oxidases are one of the most widely distributed classes of “Type-2” copper enzyme.
David M. Dooley +9 more
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Inhibition of six copper-containing amine oxidases by the antidepressant drug tranylcypromine
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Potential inhibitory effects of the clinically utilized monoamine oxidase inhibitor tranylcypromine (TCP) on mammalian, plant, bacterial, and fungal copper-containing amine oxidases have been examined. The following enzymes have been investigated: human kidney diamine oxidase (HKAO), bovine plasma amine oxidase (BPAO), equine plasma amine oxidase (EPAO)
Eric M, Shepard +3 more
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Characterization of the copper-containing amine oxidase from Trifolium pratense seedlings
Nuclear Science and Techniques, 2016We studied the kinetic characterizations of the Trifolium pratense seedlings copper-containing amine oxidase (TPAO) by using various amine-containing substrates. The catalyzing rate for all of amine-containing substrates can be ordered as diamines > polyamines > aromatic monoamines, and it shows an apparent trend in each category of substrates such as ...
Yong-Ming Zhang +5 more
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Hydroxyl radical production in the reactions of copper-containing amine oxidases with substrates
Biochimica et Biophysica Acta (BBA) - General Subjects, 1993Solutions of porcine kidney diamine oxidase, PKDAO, and bovine plasma amine oxidase, BPAO, were saturated with the spin-trapping agent alpha-phenyl-N-t-butylnitrone, PBN, and incubated with cadaverine or benzylamine substrate, respectively, under aerobic conditions.
F N, Castellano, Z, He, F T, Greenaway
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Irreversible inhibition of pig kidney copper‐containing amine oxidase by sodium and lithium ions
European Journal of Biochemistry, 2001Copper amine oxidase was found to be inhibited in a complex way by small alkali metal ions. Classic enzyme kinetic studies showed that Li+ and Na+ were weak noncompetitive inhibitors, whereas the larger alkali metals K+, Rb+ and Cs+ were not inhibitors.
PADIGLIA, ALESSANDRA +8 more
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Inhibition of copper-containing amine oxidases by Cu(II) complexes and anions
Journal of Molecular Catalysis, 1984As part of an effort to elucidate the mechanism of O2 reduction by amine oxidases and the role of copper in the overall reaction, inhibition by Cu(II) complexes and anions has been investigated. Copper(II) complexes of 1,10-phenanthroline and 2,2'-bipyridine strongly inhibited both beef plasma and pig kidney amine oxidase.
David M. Dooley +2 more
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