| Attributes | Values |
|---|
| rdf:type
| |
| Description
| - The maize Zm-p60.1 gene encodes a b-glucosidase that can release active cytokinins from their storage forms, cytokinin-O-glucosides. Mature catalytically active Zm-p60.1 is a homodimer containing five cysteine residues per a subunit. High sensitivity of the enzyme to inhibition by Ag+ or Hg2+ ions together with loss of enzyme activity upon treatment with alkylating agents indicates that a free sulfhydryl group is required for enzyme activity. Site directed mutagenesis followed by enzyme kinetic analysis suggested that cysteine residue in position 479 (C479) provides the sulfhydryl group required for enzyme activity (1). Here we report data confirming that C479 is the target for Ag+ and alkylation agent action. When the wild type enzyme was incubated in the presence of 0.5 to 128 mM silver nitrate, almost complete loss of activity was observed at 32 mM AgNO3. Mutations leading to substitutions of C479 by alanine (A), serine (S), arginine (R) or aspartic acid (D) residues resulted in a dramatic drop in
- The maize Zm-p60.1 gene encodes a b-glucosidase that can release active cytokinins from their storage forms, cytokinin-O-glucosides. Mature catalytically active Zm-p60.1 is a homodimer containing five cysteine residues per a subunit. High sensitivity of the enzyme to inhibition by Ag+ or Hg2+ ions together with loss of enzyme activity upon treatment with alkylating agents indicates that a free sulfhydryl group is required for enzyme activity. Site directed mutagenesis followed by enzyme kinetic analysis suggested that cysteine residue in position 479 (C479) provides the sulfhydryl group required for enzyme activity (1). Here we report data confirming that C479 is the target for Ag+ and alkylation agent action. When the wild type enzyme was incubated in the presence of 0.5 to 128 mM silver nitrate, almost complete loss of activity was observed at 32 mM AgNO3. Mutations leading to substitutions of C479 by alanine (A), serine (S), arginine (R) or aspartic acid (D) residues resulted in a dramatic drop in (en)
- The maize Zm-p60.1 gene encodes a b-glucosidase that can release active cytokinins from their storage forms, cytokinin-O-glucosides. Mature catalytically active Zm-p60.1 is a homodimer containing five cysteine residues per a subunit. High sensitivity of the enzyme to inhibition by Ag+ or Hg2+ ions together with loss of enzyme activity upon treatment with alkylating agents indicates that a free sulfhydryl group is required for enzyme activity. Site directed mutagenesis followed by enzyme kinetic analysis suggested that cysteine residue in position 479 (C479) provides the sulfhydryl group required for enzyme activity (1). Here we report data confirming that C479 is the target for Ag+ and alkylation agent action. When the wild type enzyme was incubated in the presence of 0.5 to 128 mM silver nitrate, almost complete loss of activity was observed at 32 mM AgNO3. Mutations leading to substitutions of C479 by alanine (A), serine (S), arginine (R) or aspartic acid (D) residues resulted in a dramatic drop in (cs)
|
| Title
| - Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment.
- Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment. (en)
- Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment. (cs)
|
| skos:prefLabel
| - Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment.
- Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment. (en)
- Identification of a Cysteine Residue Conferring Sensitivity of a Maize â-Glukosidase to Silver Ion and Alkylation Treatment. (cs)
|
| skos:notation
| - RIV/00216224:14310/01:00006022!RIV08-MSM-14310___
|
| http://linked.open.../vavai/riv/strany
| |
| http://linked.open...avai/riv/aktivita
| |
| http://linked.open...avai/riv/aktivity
| - P(VS96096), Z(MSM 143100008)
|
| 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
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/01:00006022
|
| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - Maize b-glucosidase; cysteine residues; thioredoxin fusion (en)
|
| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...v/mistoKonaniAkce
| - February 14, 2001, Brno, Czech Republic
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| http://linked.open...i/riv/mistoVydani
| |
| http://linked.open...i/riv/nazevZdroje
| - V. Pracovní setkání biochemiků a molekulárních biologů, Sborník příspěvků, Brno 2001
|
| 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...iv/tvurceVysledku
| - Zouhar, Jan
- Brzobohatý, Břetislav
- Slaný, Michal
|
| http://linked.open...vavai/riv/typAkce
| |
| http://linked.open.../riv/zahajeniAkce
| |
| http://linked.open...n/vavai/riv/zamer
| |
| number of pages
| |
| http://purl.org/ne...btex#hasPublisher
| - Masarykova univerzita v Brně
|
| https://schema.org/isbn
| |
| http://localhost/t...ganizacniJednotka
| |
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