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rdf:type
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Description
| - b-Glucosidases such as Zm-p60.1 (Zea mays) and Bgl4:1 (Brassica napus) have implicated roles in regulating plant development by releasing biologically active cytokinins from O-glucosides. A key determinant of substrate specificity in Zm-p60.1 is the F193--F200--W373--F461 cluster. However, despite sharing the same substrates, amino acids in the active sites of Zm-p60.1 and Bgl4:1 differ dramatically. In members of the Brassicaceae we found a group of b-glucosidases sharing both high similarity to Bgl4:1 and a consensus motif A-K-K-L corresponding to the F193--F200--W373-- F461 cluster. To study the mechanism of substrate specificity further, we generated and analyzed four single (F193A, F200K, W373K and F461L) and one quadruple (F193A--F200K--W373K--F461L) mutants of Zm-p60.1. The F193A mutant showed a specific increase in affinity for a small polar aglycone, and a deep decrease in kcat compared with the wild-type. Formation of a cavity with decreased hydrophobicity, and significant conse
- b-Glucosidases such as Zm-p60.1 (Zea mays) and Bgl4:1 (Brassica napus) have implicated roles in regulating plant development by releasing biologically active cytokinins from O-glucosides. A key determinant of substrate specificity in Zm-p60.1 is the F193--F200--W373--F461 cluster. However, despite sharing the same substrates, amino acids in the active sites of Zm-p60.1 and Bgl4:1 differ dramatically. In members of the Brassicaceae we found a group of b-glucosidases sharing both high similarity to Bgl4:1 and a consensus motif A-K-K-L corresponding to the F193--F200--W373-- F461 cluster. To study the mechanism of substrate specificity further, we generated and analyzed four single (F193A, F200K, W373K and F461L) and one quadruple (F193A--F200K--W373K--F461L) mutants of Zm-p60.1. The F193A mutant showed a specific increase in affinity for a small polar aglycone, and a deep decrease in kcat compared with the wild-type. Formation of a cavity with decreased hydrophobicity, and significant conse (en)
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Title
| - Functional analysis of the aglycone-binding site of the maize b-glucosidase Zm-p60.1
- Functional analysis of the aglycone-binding site of the maize b-glucosidase Zm-p60.1 (en)
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skos:prefLabel
| - Functional analysis of the aglycone-binding site of the maize b-glucosidase Zm-p60.1
- Functional analysis of the aglycone-binding site of the maize b-glucosidase Zm-p60.1 (en)
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skos:notation
| - RIV/62156489:43210/08:00132731!RIV10-MSM-43210___
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/62156489:43210/08:00132731
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - substrate specificity; Zea mays; aglycone-binding; Brassica napus; b-glucosidase (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - GB - Spojené království Velké Británie a Severního Irska
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Damborský, Jiří
- Dopitová, Radka
- Janda, Lubomír
- Jeřábek, Petr
- Brzobohatý, Břetislav
- Filipi, Tomáš
- Mazura, Pavel
- Kiran, Nagavalli Subbanna
- Chaloupkova, R.
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issn
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number of pages
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http://localhost/t...ganizacniJednotka
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