About: Functional analysis of the aglycone-binding site of the maize b-glucosidase Zm-p60.1

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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)
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)
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)
skos:notation	RIV/62156489:43210/08:00132731!RIV10-MSM-43210___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(1M06030), P(LC06034)
http://linked.open...iv/cisloPeriodika	24
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Janda, Lubomír Filipi, Tomáš Mazura, Pavel Brzobohatý, Břetislav Kiran, Nagavalli Subbanna
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Mendelova univerzita v Brně / Agronomická fakulta
http://linked.open...dnocenehoVysledku	368671
http://linked.open...ai/riv/idVysledku	RIV/62156489:43210/08:00132731
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	substrate specificity; Zea mays; aglycone-binding; Brassica napus; b-glucosidase (en)
http://linked.open.../riv/klicoveSlovo	Brassica napus substrate specificity Zea mays aglycone-binding b-glucosidase
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[3F617E75E2C2]
http://linked.open...i/riv/nazevZdroje	FEBS journal
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	5 (xsd:int)
http://linked.open...cetTvurcuVysledku	9 (xsd:int)
http://linked.open...vavai/riv/projekt	Regulation of morphogenesis of plant cells and organs Functional genomics and proteomics for crop improvement
http://linked.open...UplatneniVysledku	2008
http://linked.open...v/svazekPeriodika	275
http://linked.open...iv/tvurceVysledku	Damborský, Jiří Dopitová, Radka Janda, Lubomír Jeřábek, Petr Brzobohatý, Břetislav Filipi, Tomáš Mazura, Pavel Kiran, Nagavalli Subbanna Chaloupkova, R.
issn	1742-464X
number of pages	13 (xsd:int)
http://localhost/t...ganizacniJednotka	43210
is http://linked.open...avai/riv/vysledek of	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 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

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