COPPER BINDING SITE IN SERUM AMINE OXIDASE TREATED WITH SODIUM DIETHYLDITHIOCARBAMATE
نویسندگان
چکیده
منابع مشابه
Structural studies of copper amine oxidase
Introduction Copper amine oxidases are ubiquitous metalloenzymes. Their function in prokaryotes and lower eukaryotes is to utilise amines as a source for carbon and nitrogen. In higher eukaryotes, their roles are less well understood, but have been linked with cell signalling, growth and development, and cell death. Despite this apparent diversity, their fundamental role is to catalyse the oxid...
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Semicarbazide-sensitive amine oxidases (SSAO) are enzymes that are capable of deaminating primary amines to produce aldehyde, ammonia, and hydrogen peroxide. This activity has been associated with vascular adhesion protein-1 (VAP-1) and is found in the serum, endothelium, adipose, and smooth muscle of mammals. Circulating SSAO activity is increased in congestive heart failure, diabetes, and inf...
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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). Following the formation of aldehyde, the enz...
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The toxicity of extracellular spermine, determined in the presence of fetal calf serum, was studied using three cell lines: FM3A, L1210, and NIH3T3 cells. Amine oxidase in fetal calf serum produces aminodialdehyde generating acrolein spontaneously, H(2)O(2), and ammonia from spermine. Spermine toxicity was prevented by aldehyde dehydrogenase, but not by catalase. Similar concentrations of sperm...
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ژورنال
عنوان ژورنال: Chemistry Letters
سال: 1982
ISSN: 0366-7022,1348-0715
DOI: 10.1246/cl.1982.487