Results 181 to 190 of about 22,060 (235)

Structural organization of mammalian copper-containing amine oxidase genes

Inflammation Research, 2009
Analysis 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 ...
H G Schwelberger
exaly   +3 more sources

Guanabenz as inhibitor of copper-containing amine oxidases

Agents and Actions, 1986
The 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, B, Bertocci, L, Raimondi, G, Soldani, M, Del Tacca, F, Buffoni   +5 more
openaire   +2 more sources

Copper-Containing Amine Oxidases

2020
The 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
openaire   +1 more source

Inactivation of copper‐containing amine oxidases by turnover products

European Journal of Biochemistry, 2003
For 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, S. NOCERA, R. FEDERICO, MONDOVI', Bruno, L. MORPURGO   +4 more
openaire   +4 more sources

Substrate specificity of copper-containing plant amine oxidases

Journal of Inorganic Biochemistry, 2007
The 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, R. Federico, MONDOVI', Bruno, L. Morpurgo   +3 more
openaire   +4 more sources

Biochemical aspects and functional role of the copper-containing amine oxidases

InflammoPharmacology, 2003
The 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
openaire   +2 more sources

Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective

Archives of Biochemistry and Biophysics, 2004
This 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, Bryan J, Johnson, Carrie M, Wilmot   +2 more
openaire   +2 more sources

Oxygen activation in a copper-containing amine oxidase

Biochemical Society Transactions, 2003
The 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 ...
openaire   +2 more sources

Crystallization and Preliminary Crystallographic Characterization of the Copper-containing Amine Oxidase from Pea Seedlings

Journal of Molecular Biology, 1993
The copper-containing amine oxidase from pea seedlings has been crystallized using lithium sulfate as precipitant at pH 5.2. The unit cell is orthorhombic, space group P2(1)2(1)2(1), with dimensions a = 89.3 A, b = 113.4 A, c = 199.0 A. The mass of the asymmetric unit is 131(+/- 13) kDa, consistent with independent evidence that the molecule has two ...
D M Dooley, J Mitchell Guss, Michele A Mcguirl   +2 more
exaly   +3 more sources