About: Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst

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About: Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst Goto Sponge NotDistinct Permalink

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Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://glycob.oxfordjournals.org/content/24/12/1301.long
Description	This study is focused on the analysis and mutagenesis of beta-mannosidase from Bacteroides thetaiotaomicron with the aim of broadening its substrate specificity to 2-acetamido-2-deoxy-beta-d-mannopyranosyl (beta-ManNAc) derivatives. Various conformations (4C1, 4H5, and 1S5) of native and modified ligands were docked to the binding site of the protein to determine the most suitable conformation of sugars for further hydrolysis. Key amino acid residues were mutated in silico focusing on stabilizing the acetamido group of beta-ManNAc as well as forming the oxazoline intermediate needed for hydrolysis. The results of large set of 5 ns molecular dynamic simulations showed that the majority of the active site residues are involved in substrate interaction and do not exhibit a higher flexibility except for Asn178. Mutations of Asn178 to alanine and Asp199 to serine could lead to a stabilisation of the acetamido group in the binding site. This study is focused on the analysis and mutagenesis of beta-mannosidase from Bacteroides thetaiotaomicron with the aim of broadening its substrate specificity to 2-acetamido-2-deoxy-beta-d-mannopyranosyl (beta-ManNAc) derivatives. Various conformations (4C1, 4H5, and 1S5) of native and modified ligands were docked to the binding site of the protein to determine the most suitable conformation of sugars for further hydrolysis. Key amino acid residues were mutated in silico focusing on stabilizing the acetamido group of beta-ManNAc as well as forming the oxazoline intermediate needed for hydrolysis. The results of large set of 5 ns molecular dynamic simulations showed that the majority of the active site residues are involved in substrate interaction and do not exhibit a higher flexibility except for Asn178. Mutations of Asn178 to alanine and Asp199 to serine could lead to a stabilisation of the acetamido group in the binding site. (en)
Title	Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst (en)
skos:prefLabel	Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst Protein engineering study of beta-mannosidase to set up a potential chemically efficient biocatalyst (en)
skos:notation	RIV/00216224:14740/14:00073772!RIV15-MSM-14740___
http://linked.open...avai/riv/aktivita	I P S
http://linked.open...avai/riv/aktivity	I, P(7E11011), P(ED1.1.00/02.0068), P(GAP207/10/0321), S
http://linked.open...iv/cisloPeriodika	12
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Demo, Gabriel Štěpán, Jakub Koča, Jaroslav Wimmerová, Michaela Horská, Veronika
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	Masarykova univerzita / Středoevropský technologický institut
http://linked.open...dnocenehoVysledku	40471
http://linked.open...ai/riv/idVysledku	RIV/00216224:14740/14:00073772
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Docking beta-mannosidase molecular dynamics mutagenesis protein engineering (en)
http://linked.open.../riv/klicoveSlovo	Docking beta-mannosidase molecular dynamics mutagenesis protein engineering
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[02D8F97676D1]
http://linked.open...i/riv/nazevZdroje	Glycobiology
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	5 (xsd:int)
http://linked.open...cetTvurcuVysledku	8 (xsd:int)
http://linked.open...vavai/riv/projekt	Central european institute of technology Novel Biocatalysts for the Production of Glycosides The ways to N-acetyl-mannosamine structures via mannoside metabolizing enzymes
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	24
http://linked.open...iv/tvurceVysledku	Demo, Gabriel Koča, Jaroslav Křen, Vladimír Wimmerová, Michaela Štěpán, Jakub Weignerova, Lenka Horská, Veronika Fliedrova, Barbora
http://linked.open...ain/vavai/riv/wos	000347410300011
issn	0959-6658
number of pages	11 (xsd:int)
http://bibframe.org/vocab/doi	10.1093/glycob/cwu074
http://localhost/t...ganizacniJednotka	14740

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