About: Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis

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About: Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Using changes in intrinsic tryptophan fluorescence to determine the affinity of human BHMT for substrates, products, or CBHcy, we now demonstrate that the enzyme-substrate complex reaches its transition state through an ordered bi-bi mechanism in which Hcy is the first substrate to bind and Met is the last product released Using changes in intrinsic tryptophan fluorescence to determine the affinity of human BHMT for substrates, products, or CBHcy, we now demonstrate that the enzyme-substrate complex reaches its transition state through an ordered bi-bi mechanism in which Hcy is the first substrate to bind and Met is the last product released (en) Stanovení afinity lidské BHMT k substrátům, produktům a CBHcy pomocí změn vnitřní tryptofanové fluorescence ukázalo, že komplex enzym-substrát se dostává do tranzitního stavu uspořádaným bi-bi mechanismem, ve kterém se Hcy váže na enzym jako první substrát a Met je posledním uvolněným produktem (cs)
Title	Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis Analýza katalytického mechanismu betain-homocystein S-metyltransferázy pomocí vnitřní tryptofanové fluorescence a místně cílené metageneze (cs) Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis (en)
skos:prefLabel	Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis Analýza katalytického mechanismu betain-homocystein S-metyltransferázy pomocí vnitřní tryptofanové fluorescence a místně cílené metageneze (cs) Dissecting the Catalytic Mechanism of Betaine - Homocysteine S-Methyltransferase by Use of Intrinsic Tryptophan Fluorescence and Site-Directed Mutagenesis (en)
skos:notation	RIV/61388963:_____/04:00100811!RIV/2005/AV0/A57005/N
http://linked.open.../vavai/riv/strany	5341;5351
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(IAA4055302), Z(AV0Z4055905)
http://linked.open...iv/cisloPeriodika	18
http://linked.open...vai/riv/dodaniDat	2005
http://linked.open...aciTvurceVysledku	Jiráček, Jiří Collinsová, Michaela
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	Ústav organické chemie a biochemie AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	560795
http://linked.open...ai/riv/idVysledku	RIV/61388963:_____/04:00100811
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	BHMT;CBHcy;fluorescence (en)
http://linked.open.../riv/klicoveSlovo	fluorescence CBHcy BHMT
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[B3557C2BDD31]
http://linked.open...i/riv/nazevZdroje	Biochemistry
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	7 (xsd:int)
http://linked.open...vavai/riv/projekt	Transition-state mimicking inhibitors of human betaine: homocysteine S-methyltransferase
http://linked.open...UplatneniVysledku	2004
http://linked.open...v/svazekPeriodika	43
http://linked.open...iv/tvurceVysledku	Jiráček, Jiří Garrow, T. A. Collinsová, Michaela Castro, C. Evans, J. C. Ludwig, M. L. Gratson, A. A.
http://linked.open...n/vavai/riv/zamer	Chemical principles of selected biological phenomena in medicine and ecology
issn	0006-2960
number of pages	11 (xsd:int)

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