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Protein-derived cofactors: chemical innovations expanding enzyme catalysis.
Chem Soc RevGraciano A, Liu A.
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Structural organization of mammalian copper-containing amine oxidase genes
Inflammation Research, 2009Analysis of sequence conservation and structural organization of mammalian genes encoding copper-containing amine oxidases (CAO).Sequences of previously characterized genes encoding CAO proteins were used to identify homologous mammalian genes in the NCBI genome sequence databases and to analyze sequence and structural conservation of these genes ...
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Irreversible inhibition of pig kidney copper-containing amine oxidase by sodium and lithium ions
FEBS Journal, 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.
Maurizio Paci +2 more
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Copper-Containing Amine Oxidases
2020The three new cofactors are 2,4'-bitryptophan-6',7'-dione in methylamine dehydrogenase, 3'-S-cysteinyltyrosine in galactose oxidase and 6-hydroxydopa quinone, or topa quinone in copper-containing amine oxidases. Copper-containing amine oxidases are distinct from other mammalian amine oxidases.
William S. Mclntire, Christa Hartmann
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Guanabenz as inhibitor of copper-containing amine oxidases
Agents and Actions, 1986The effects of guanabenz on some copper containing amine oxidases are described. Guanabenz 'in vitro' inhibits pig plasma benzylamine oxidase with a IC50 M 5.1 +/- 0.8 X 10(-6) M. It also inhibits pig kidney diamine oxidase and rat liver mitochondrial monoamine oxidase at higher concentrations.
G, Banchelli +5 more
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Inactivation of copper‐containing amine oxidases by turnover products
European Journal of Biochemistry, 2003For bovine serum amine oxidase, two different mechanisms of substrate‐induced inactivation have been proposed. One consists of a slow oxidation by H2O2 of a conserved residue in the reduced enzyme after the fast turnover phase [Pietrangeli, P., Nocera, S., Fattibene, P., Wang, X.T., Mondovì, B. & Morpurgo, L. (2000) Biochem. Biophys. Res.
PIETRANGELI, Paola +4 more
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Substrate specificity of copper-containing plant amine oxidases
Journal of Inorganic Biochemistry, 2007The steady-state kinetic parameters of the amine oxidases purified from Lathyrus cicera (LCAO) and Pisum sativum (PSAO) seedling were measured on a series of common substrates, previously tested on bovine serum amine oxidase (BSAO). LCAO, as PSAO, was substantially more reactive than BSAO with aliphatic diamines and histamine.
PIETRANGELI, Paola +3 more
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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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Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective
Archives of Biochemistry and Biophysics, 2004This review will focus on how X-ray crystallographic studies of copper-containing amine oxidases have complemented the solution, kinetic, and spectroscopic research on this ubiquitous class of enzymes. These enzymes not only contain a copper ion at the active site, but also a unique organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ), which ...
Brian J, Brazeau +2 more
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