About: Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

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About: Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	The characterization of the PsAMADH2 proteins, altered here by site-directed mutagenesis, suggests that the D110 and D113 residues at the entrance to the substrate channel are required for high-affinity binding of omega-aminoaldehydes to PsAMADH2 and for enzyme activity, whereas N162, near catalytic C294, contributes mainly to the enzyme's catalytic rate. Inside the substrate cavity, W170 and Y163, and, to a certain extent, L166 and M167 probably preserve the optimal overall geometry of the substrate channel that allows for the appropriate orientation of the substrate. Unconserved W288 appears to affect the affinity of the enzyme for the substrate amino group through control of the substrate channel diameter without affecting the reaction rate. Therefore, W288 may be a key determinant of the differences in substrate specificity found among plant AMADH isoforms when they interact with naturally occurring substrates such as 3-aminopropionaldehyde and 4-aminobutyraldehyde. The characterization of the PsAMADH2 proteins, altered here by site-directed mutagenesis, suggests that the D110 and D113 residues at the entrance to the substrate channel are required for high-affinity binding of omega-aminoaldehydes to PsAMADH2 and for enzyme activity, whereas N162, near catalytic C294, contributes mainly to the enzyme's catalytic rate. Inside the substrate cavity, W170 and Y163, and, to a certain extent, L166 and M167 probably preserve the optimal overall geometry of the substrate channel that allows for the appropriate orientation of the substrate. Unconserved W288 appears to affect the affinity of the enzyme for the substrate amino group through control of the substrate channel diameter without affecting the reaction rate. Therefore, W288 may be a key determinant of the differences in substrate specificity found among plant AMADH isoforms when they interact with naturally occurring substrates such as 3-aminopropionaldehyde and 4-aminobutyraldehyde. (en)
Title	Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases (en)
skos:prefLabel	Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases (en)
skos:notation	RIV/61989592:15310/11:10223645!RIV12-MSM-15310___
http://linked.open...avai/predkladatel	Přírodovědecká fakulta
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(ED0007/01/01), P(GA522/08/0555), P(GAP501/11/1591), Z(MSM6198959215)
http://linked.open...iv/cisloPeriodika	17
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Tylichová, Martina Kopečný, David Šebela, Marek
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	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	189167
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/11:10223645
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	3-aminopropionaldehyde, 4-aminobutyraldehyde, 4-guanidinobutyraldehyde, aminoaldehyde dehydrogenase, betaine aldehyde (en)
http://linked.open.../riv/klicoveSlovo	3-aminopropionaldehyde 4-aminobutyraldehyde 4-guanidinobutyraldehyde aminoaldehyde dehydrogenase betaine aldehyde
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[900FEF5C64D7]
http://linked.open...i/riv/nazevZdroje	F E B S Journal
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Centre of the Region Haná for Biotechnological and Agricultural Research Structure-functional characterization of oxidoreductases acting on nitrogenous regulatory compounds in plants Structure-functional characterization of selected plant aldehyde dehydrogenases
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	278
http://linked.open...iv/tvurceVysledku	Kopečný, David Popelková, Hana Snégaroff, Jacques Tylichová, Martina Šebela, Marek
http://linked.open...ain/vavai/riv/wos	000294025800016
http://linked.open...n/vavai/riv/zamer	Variabilita složek a interakcí v rostlinném patosystému a vliv faktorů prostředí na jejich projev
issn	1742-464X
number of pages	10 (xsd:int)
http://bibframe.org/vocab/doi	10.1111/j.1742-4658.2011.08239.x
http://localhost/t...ganizacniJednotka	15310
is http://linked.open...avai/riv/vysledek of	Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases Carboxylate and aromatic active-site residues are determinants of high-affinity binding of omega-aminoaldehydes to plant aminoaldehyde dehydrogenases

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