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Description
  • Tato kapitola v knize se zabývá enzymy aminoxidasami (EC 1.4.3.6), které se podílejí na degradaci buněčných regulátorů polyaminů. Přehledně jsou shrnuty vlastnosti těchto enzymů a jejich fyziologické funkce. Jsou rovněž diskutovány další směry možného výzkumu aminoxidas a možnost i praktické aplikace enzymů. (cs)
  • Amine oxidases (EC 1.4.3.6) that contain copper/topa quinone cofactor belong to a new protein group of quinoproteins emerging in recentyears. This review brings together information on the general properties of the enzymes and their physiological functions. In plants, these enzymes are involved in processes of development and senescence, they reduce the concentration of toxic amines produced during exposure to stress conditions, provide hydrogen peroxide for wall stiffening and lignification and precursor compounds for biosynthesis of some alkaloids. Major attention is currently being paid to the structure of the active site of the enzymes that contains copper ions and a posttranslationally modified tyrosyl residue, topa quinone. Three-dimensional structures recently obtained for several amine oxidases by X-ray diffraction analysis of the respective crystals provide important structural information about the unique protein folding of the native enzyme and molecular arrangement of the active site. Bi
  • Amine oxidases (EC 1.4.3.6) that contain copper/topa quinone cofactor belong to a new protein group of quinoproteins emerging in recentyears. This review brings together information on the general properties of the enzymes and their physiological functions. In plants, these enzymes are involved in processes of development and senescence, they reduce the concentration of toxic amines produced during exposure to stress conditions, provide hydrogen peroxide for wall stiffening and lignification and precursor compounds for biosynthesis of some alkaloids. Major attention is currently being paid to the structure of the active site of the enzymes that contains copper ions and a posttranslationally modified tyrosyl residue, topa quinone. Three-dimensional structures recently obtained for several amine oxidases by X-ray diffraction analysis of the respective crystals provide important structural information about the unique protein folding of the native enzyme and molecular arrangement of the active site. Bi (en)
Title
  • Copper/topa quinone-containing amine oxidases - recent research developments
  • Copper/topa quinone-containing amine oxidases - recent research developments (en)
  • Aminoxidasy obsahující měď a topachinon - nejnovější výsledky (cs)
skos:prefLabel
  • Copper/topa quinone-containing amine oxidases - recent research developments
  • Copper/topa quinone-containing amine oxidases - recent research developments (en)
  • Aminoxidasy obsahující měď a topachinon - nejnovější výsledky (cs)
skos:notation
  • RIV/61989592:15310/02:00007750!RIV09-MSM-15310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(ME 153), Z(MSM 153100010)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 641780
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/02:00007750
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • amine oxidase; topa quinone; copper (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [1C9B9589725E]
http://linked.open...i/riv/mistoVydani
  • Amsterdam
http://linked.open...i/riv/nazevZdroje
  • Studies in Natural Products Chemistry, Vol. 26
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...v/pocetStranKnihy
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Petřivalský, Marek
  • Šebela, Marek
  • Frébort, Ivo
  • Peč, Pavel
http://linked.open...n/vavai/riv/zamer
number of pages
http://purl.org/ne...btex#hasPublisher
  • Elsevier
https://schema.org/isbn
  • 0-444-51004-4
http://localhost/t...ganizacniJednotka
  • 15310
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