About: High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • Enzym cytokinin oxidasa/dehydrogenasa (CKO/CKX) z kukuřice byl připraven jako rekombinantní protein v hostitelské kvasince Yarrowia lipolytica. Rekombinantní enzym byl izolován z kultury transformovaných kvasinek a přečištěn do homogenního stavu. Následně byly charakterizovány molekulové a kinetické vlastnosti enzymu. (cs)
  • Cytokinin oxidase/dehydrogenase (CKO/CKX) is a flavoenzyme, which irreversibly inactivates cytokinins by severing the isoprenoid side chain from the adenine/adenosine moiety. There are several genes coding for the enzyme in maize (Zea mays). A Z. mays CKO1 cDNA was cloned in the yeast Yarrowia lipolytica to achieve heterologous protein expression. The recombinant ZmCKO1 was recovered from cultures of transformed yeasts and purified using several chromatographic steps. The enzyme was obtained as a homogeneous protein in a remarkably high-yield and its molecular and kinetic properties were characterized. The enzyme showed a molecular mass of 69 kDa, pI was 6.3. Neutral sugar content of the molecule was 22%. Absorption and fluorescence spectra were in accordance with the presence of FAD as a cofactor. Peptide mass fingerprinting using MALDI-MS correctly assigned the enzyme in MSDB protein database. The enzyme showed a relatively high degree of thermostability (T50 = 55 °C for 30 min incubation). The foll
  • Cytokinin oxidase/dehydrogenase (CKO/CKX) is a flavoenzyme, which irreversibly inactivates cytokinins by severing the isoprenoid side chain from the adenine/adenosine moiety. There are several genes coding for the enzyme in maize (Zea mays). A Z. mays CKO1 cDNA was cloned in the yeast Yarrowia lipolytica to achieve heterologous protein expression. The recombinant ZmCKO1 was recovered from cultures of transformed yeasts and purified using several chromatographic steps. The enzyme was obtained as a homogeneous protein in a remarkably high-yield and its molecular and kinetic properties were characterized. The enzyme showed a molecular mass of 69 kDa, pI was 6.3. Neutral sugar content of the molecule was 22%. Absorption and fluorescence spectra were in accordance with the presence of FAD as a cofactor. Peptide mass fingerprinting using MALDI-MS correctly assigned the enzyme in MSDB protein database. The enzyme showed a relatively high degree of thermostability (T50 = 55 °C for 30 min incubation). The foll (en)
Title
  • High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
  • Vysokoúrovňová exprese a charakterizace cytokininoxidasy/dehydrogenasy ze Zea mays v Yarrowia lipolytica (cs)
  • High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica (en)
skos:prefLabel
  • High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
  • Vysokoúrovňová exprese a charakterizace cytokininoxidasy/dehydrogenasy ze Zea mays v Yarrowia lipolytica (cs)
  • High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica (en)
skos:notation
  • RIV/61989592:15310/05:00002162!RIV06-MSM-15310___
http://linked.open.../vavai/riv/strany
  • 1011-1022
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(ME 664), Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika
  • 11
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
  • 523305
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/05:00002162
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • POLYACRYLAMIDE-GELS; POLYAMINE OXIDASE; YEAST; DEHYDROGENASE; PURIFICATION; PROTEINS; DEGRADATION; CLONING; MAIZE; ACID (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • FR - Francouzská republika
http://linked.open...ontrolniKodProRIV
  • [395AF61762E6]
http://linked.open...i/riv/nazevZdroje
  • Biochimie
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 87
http://linked.open...iv/tvurceVysledku
  • Kopečný, David
  • Šebela, Marek
  • Madzak, Catherine
  • Houba-Hérin, Nicole
  • Laloue, Michel
  • Majira, Amel
  • Pethe, Claude
http://linked.open...n/vavai/riv/zamer
issn
  • 0300-9084
number of pages
http://localhost/t...ganizacniJednotka
  • 15310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 67 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software