About: Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu     Goto   Sponge   NotDistinct   Permalink

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Description
  • Cu-amine oxidases (CAOs) catalyze the oxidative deamination of biogenic amines. An amine, oxygen and water enter into the reaction and the products are corresponding aldehyde, ammonia and hydrogen peroxide. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) belongs to a group of microbial Cu-amine oxidases. The best substrates are 2-phenylethylamine and tyramine. Three types of AGAO have been studied. %22Wild type%22, i.e. native holoenzyme, and its two mutants K184Q and K354Q, where lysine is replaced with glutamine. These mutants have the same catalytic activity as the %22wild type%22. All three types were provided by prof. Katsuyuki Tanizawa from Institute for Industrial Research, Osaka University, Japan. The main goal of the work was to describethe interaction of AGAO with 2-butyne-1,4-diamine (DABI), an analogue of putrescine and a typical mechanism-based inhibitor of other amine oxidases which is CAO from Pisum sativum (PSAO) 3. The formation of the aminoallenic intermediate is suggested to
  • Cu-amine oxidases (CAOs) catalyze the oxidative deamination of biogenic amines. An amine, oxygen and water enter into the reaction and the products are corresponding aldehyde, ammonia and hydrogen peroxide. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) belongs to a group of microbial Cu-amine oxidases. The best substrates are 2-phenylethylamine and tyramine. Three types of AGAO have been studied. %22Wild type%22, i.e. native holoenzyme, and its two mutants K184Q and K354Q, where lysine is replaced with glutamine. These mutants have the same catalytic activity as the %22wild type%22. All three types were provided by prof. Katsuyuki Tanizawa from Institute for Industrial Research, Osaka University, Japan. The main goal of the work was to describethe interaction of AGAO with 2-butyne-1,4-diamine (DABI), an analogue of putrescine and a typical mechanism-based inhibitor of other amine oxidases which is CAO from Pisum sativum (PSAO) 3. The formation of the aminoallenic intermediate is suggested to (en)
Title
  • Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu
  • Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu (cs)
  • Mechanism-based inhibition of Cu-amine oxidase from the bacterium Arthrobacter globiformis in the presence of 2-butyne-1,4-diamine (en)
skos:prefLabel
  • Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu
  • Na mechanimu závislá inhibice Cu-aminoxidasy z baktérie Arthrobacter globiformis v přítomnosti 2-butyn-1,4-diaminu (cs)
  • Mechanism-based inhibition of Cu-amine oxidase from the bacterium Arthrobacter globiformis in the presence of 2-butyne-1,4-diamine (en)
skos:notation
  • RIV/61989592:15310/02:00001556!RIV/2003/MSM/153103/N
http://linked.open.../vavai/riv/strany
  • 226
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  • Z(MSM 153100010)
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  • 4
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  • 654764
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/02:00001556
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  • amine oxidase; Arthrobacter globiformis; mechanism-based inhibition (en)
http://linked.open.../riv/klicoveSlovo
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  • CZ - Česká republika
http://linked.open...ontrolniKodProRIV
  • [A6454786D19F]
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  • Chemické listy
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
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http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 96
http://linked.open...iv/tvurceVysledku
  • Šebela, Marek
  • Frébort, Ivo
  • Peč, Pavel
  • Tanizawa, Katsuyuki
  • Brauner, František
  • Lamplot, Zbyněk
http://linked.open...n/vavai/riv/zamer
issn
  • 0009-2770
number of pages
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  • 15310
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