About: Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni     Goto   Sponge   NotDistinct   Permalink

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Description
  • Comamonas testosteroni Pb50 is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This bacterial strain is capable of utilizing phenol as the sole carbon and energy source. Although examples are known in which the C. testosteroni utilizes phenol for growth or metabolism, much less information are known on the nature of the phenol-oxidizing enzymes in this microorganism. Therefore, the occurrence and cellular location of phenol hydroxylase (EC 1.14.13.7), the enzyme participating in the first step of phenol degradation, catalyzing its hydroxylation to catechol in a bacterial Comamonas testosteroni Pb50 strain grown in the presence of phenol as a sole carbon and energy source are the aims of this study.
  • Comamonas testosteroni Pb50 is a microorganism that possesses high tolerance for phenol and shows strong phenol degrading activity. This bacterial strain is capable of utilizing phenol as the sole carbon and energy source. Although examples are known in which the C. testosteroni utilizes phenol for growth or metabolism, much less information are known on the nature of the phenol-oxidizing enzymes in this microorganism. Therefore, the occurrence and cellular location of phenol hydroxylase (EC 1.14.13.7), the enzyme participating in the first step of phenol degradation, catalyzing its hydroxylation to catechol in a bacterial Comamonas testosteroni Pb50 strain grown in the presence of phenol as a sole carbon and energy source are the aims of this study. (en)
Title
  • Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni
  • Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni (en)
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  • Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni
  • Isolation and partial characterization of extracellular NADPH-dependent phenol hydroxylase oxidizing phenol to catechol in Comamonas testosteroni (en)
skos:notation
  • RIV/00216208:11310/11:10107200!RIV12-GA0-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0505), P(GAP503/11/0163), Z(MSM0021620808)
http://linked.open...iv/cisloPeriodika
  • Suppl. 1
http://linked.open...vai/riv/dodaniDat
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  • 205913
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  • RIV/00216208:11310/11:10107200
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  • phenol hydroxylase; Comamonas testosteroni; biodegradation; phenol (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • SE - Švédské království
http://linked.open...ontrolniKodProRIV
  • [A4B9B05CF6FB]
http://linked.open...i/riv/nazevZdroje
  • Neuroendocrinology Letters
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http://linked.open...v/svazekPeriodika
  • 32
http://linked.open...iv/tvurceVysledku
  • Halecký, Martin
  • Páca, Jan
  • Stiborová, Marie
  • Kremláčková, Veronika
  • Turek, Michal
  • Vilímková, Lenka
http://linked.open...n/vavai/riv/zamer
issn
  • 0172-780X
number of pages
http://localhost/t...ganizacniJednotka
  • 11310
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