نتایج جستجو برای: copper containing amine oxidases

تعداد نتایج: 436899  

Journal: :The Journal of biological chemistry 1970
D W Reed P G Passon D E Hultquist

A previously undetected pink copper protein has been isolated from human erythrocytes and purified by chromatographic procedures. The purified protein sedimented as a single symmetrical peak in the ultracentrifuge but minor impurities were detected by polyacrylamide disc electrophoresis. The apparent molecular weight was calculated to be approximately 32,000 by both Bio-Gel P-60 chromatography ...

Journal: :Biochemical Society transactions 1992
A Messerschmidt

Introduction Ascorbic acid oxidase (AAO) is ;I blue multi-copper oxidase that catalyses the four-electron reduction of dioxygen to water with concomitant one-electron oxidation of tlie reducing organic substrate [ 1 1. Copper-dependent A A O is found only in higher plants 12 I. The enzyme from Cucurbitu pep0 medullosa (green zucchini) is ;I dimer of 14OOOO-M,. containing eight copper ions of th...

2016
Paraskevi Tavladoraki Alessandra Cona Riccardo Angelini

Plant polyamines are catabolized by two classes of amine oxidases, the copper amine oxidases (CuAOs) and the flavin adenine dinucleotide (FAD)-dependent polyamine oxidases (PAOs). These enzymes differ to each other in substrate specificity, catalytic mechanism and subcellular localization. CuAOs and PAOs contribute to several physiological processes both through the control of polyamine homeost...

Journal: :Clinical science 1999
J Ekblom J Grönvall B Lennernäs S Nilsson H Garpenstrand L Oreland

The semicarbazide-sensitive amine oxidases constitute a group of copper-containing enzymes whose physiological function is unclear. The enzymes are present in various tissues, including blood plasma. At present, the source of the plasma enzyme in humans is not known. Results of a recent study suggested that semicarbazide-sensitive amine oxidase is expressed in the skeleton, e.g. in the spine. U...

Journal: :Eukaryotic cell 2008
Chardeen Peter Julie Laliberté Jude Beaudoin Simon Labbé

Copper amine oxidases (CAOs) have been proposed to be involved in the metabolism of xenobiotic and biogenic amines. The requirement for copper is absolute for their activity. In the fission yeast Schizosaccharomyces pombe, cao1(+) and cao2(+) genes are predicted to encode members of the CAO family. While both genes are expressed in wild-type cells, we determined that the expression of only cao1...

2008
Ayse Hacisalihoglu Jaap A. Jongejan Johannis A. Duine

Department of Microbiology and Enzymology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands The bacteria Klebsiella oxytoca LMD 72.65 (ATCC 8724), Arthrobacter PI LMD 81.60 (NCIB 11 625), Paracoccus wersutus LMD 80.62 (ATCC 25364), Escherichia coli W LMD 50.28 (ATCC 9637), E. coli K12 LMD 93.68, Pseudomonas aeruginosa PA01 LMD 89.1 (ATCC 17933) and Pseudomonas puti...

Journal: :Journal of the American Chemical Society 2014
Alison E Wendlandt Shannon S Stahl

Copper amine oxidases are a family of enzymes with quinone cofactors that oxidize primary amines to aldehydes. The native mechanism proceeds via an iminoquinone intermediate that promotes high selectivity for reactions with primary amines, thereby constraining the scope of potential biomimetic synthetic applications. Here we report a novel bioinspired quinone catalyst system consisting of 1,10-...

2015
Sandip A. Ghuge Alessandra Tisi Andrea Carucci Renato A. Rodrigues-Pousada Stefano Franchi Paraskevi Tavladoraki Riccardo Angelini Alessandra Cona

Polyamines (PAs) are aliphatic polycations present in all living organisms. A growing body of evidence reveals their involvement as regulators in a variety of physiological and pathological events. They are oxidatively deaminated by amine oxidases (AOs), including copper amine oxidases (CuAOs) and flavin adenine dinucleotide (FAD)-dependent polyamine oxidases (PAOs). The biologically-active hyd...

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