Matches in SemOpenAlex for { <https://semopenalex.org/work/W2090924127> ?p ?o ?g. }
Showing items 1 to 77 of
77
with 100 items per page.
- W2090924127 endingPage "504" @default.
- W2090924127 startingPage "497" @default.
- W2090924127 abstract "Chez les plantes, le transfert de l'atome de soufre entre la cystéine et l'homocystéine, précurseur direct de la méthionine, est catalysé par deux enzymes chloroplastiques, la cystathionine γ-synthase et la cystathionine β-lyase. Ces protéines ont été purifiées à l'homogénéité à partir de chloroplastes de feuilles d'épinard et leurs propriétés biochimiques ont été définies. Ces enzymes présentent une structure tétramérique, chaque sous-unité fixant une molécule de pyridoxal 5′-phosphate comme cofacteur. De plus, la cystathionine γ-synthase et la cystathionine β-lyase sont les cibles d'inhibiteurs puissants de la synthèse de la méthionine qui sont létaux pour la plante. Un ADNc codant pour la cystathionine β-lyase chloroplastique d'Arabidopsis thaliana a été isolé par complémentation fonctionnelle d'un mutant bactérien et clone dans un vecteur de surproduction afin de transformer Escherichia coli. La caractérisation fine des interactions entre i) le pyridoxal 5′-phosphate et la chaîne polypeptidique et ii) l'inhibiteur de type substrat-suicide aminoéthoxyvinylglycine et le cofacteur lié à l'enzyme constitue une étude préliminaire du site actif de l'enzyme recombinante qui sera poursuivie par une analyse cristallographique. In plants, the transfer of the sulfur atom between cysteine and homocysteine, the direct precursor of methionine, is ensured by two chloroplastic enzymes, cystathionine γ-synthase and cystathionine β-lyase. These proteins have been purified to homogeneity from spinach chloroplasts and their biochemical properties determined. Cystathionine γ-synthase and cystathionine β-lyase are tetramers and are typical pyridoxal 5′-phosphate-dependent proteins. These enzymes are targets for the potent inhibitors of methionine synthesis that are lethal for plants. An Arabidopsis thaliana cDNA encoding chloroplastic cystathionine β-lyase was isolated by functional complementation of a bacterial mutant and cloned in a pET expression vector in order to transform Escherichia coli cells. Preliminary observations of the active site of the purified recombinant enzyme have been performed by characterization of the interaction between i) pyridoxal 5′-phosphate and the polypeptide chain, and ii) the active site-directed inhibitor aminoethoxyvinylglycine and the bound cofactor. This study will be developed further by crystallographic analyses." @default.
- W2090924127 created "2016-06-24" @default.
- W2090924127 creator A5007782541 @default.
- W2090924127 date "1997-06-01" @default.
- W2090924127 modified "2023-09-25" @default.
- W2090924127 title "Methionine biosynthesis in higher plants: biochemical and molecular characterization of the transsulfuration pathway enzymes" @default.
- W2090924127 cites W1755546657 @default.
- W2090924127 cites W1861199552 @default.
- W2090924127 cites W1972091514 @default.
- W2090924127 cites W1974302254 @default.
- W2090924127 cites W1976037543 @default.
- W2090924127 cites W1989245996 @default.
- W2090924127 cites W2009696126 @default.
- W2090924127 cites W2020335713 @default.
- W2090924127 cites W2020989044 @default.
- W2090924127 cites W2024071602 @default.
- W2090924127 cites W2036216475 @default.
- W2090924127 cites W2043339131 @default.
- W2090924127 cites W2051579324 @default.
- W2090924127 cites W2075757116 @default.
- W2090924127 cites W2079058399 @default.
- W2090924127 cites W2090058311 @default.
- W2090924127 cites W2128956788 @default.
- W2090924127 cites W2210919387 @default.
- W2090924127 cites W2319826932 @default.
- W2090924127 cites W4241771146 @default.
- W2090924127 cites W981751877 @default.
- W2090924127 doi "https://doi.org/10.1016/s0764-4469(97)81977-4" @default.
- W2090924127 hasPublicationYear "1997" @default.
- W2090924127 type Work @default.
- W2090924127 sameAs 2090924127 @default.
- W2090924127 citedByCount "4" @default.
- W2090924127 crossrefType "journal-article" @default.
- W2090924127 hasAuthorship W2090924127A5007782541 @default.
- W2090924127 hasConcept C153911025 @default.
- W2090924127 hasConcept C16525657 @default.
- W2090924127 hasConcept C181199279 @default.
- W2090924127 hasConcept C185592680 @default.
- W2090924127 hasConcept C187566844 @default.
- W2090924127 hasConcept C2777269803 @default.
- W2090924127 hasConcept C2779375456 @default.
- W2090924127 hasConcept C2780912031 @default.
- W2090924127 hasConcept C515207424 @default.
- W2090924127 hasConcept C55493867 @default.
- W2090924127 hasConcept C86803240 @default.
- W2090924127 hasConceptScore W2090924127C153911025 @default.
- W2090924127 hasConceptScore W2090924127C16525657 @default.
- W2090924127 hasConceptScore W2090924127C181199279 @default.
- W2090924127 hasConceptScore W2090924127C185592680 @default.
- W2090924127 hasConceptScore W2090924127C187566844 @default.
- W2090924127 hasConceptScore W2090924127C2777269803 @default.
- W2090924127 hasConceptScore W2090924127C2779375456 @default.
- W2090924127 hasConceptScore W2090924127C2780912031 @default.
- W2090924127 hasConceptScore W2090924127C515207424 @default.
- W2090924127 hasConceptScore W2090924127C55493867 @default.
- W2090924127 hasConceptScore W2090924127C86803240 @default.
- W2090924127 hasIssue "6" @default.
- W2090924127 hasLocation W20909241271 @default.
- W2090924127 hasOpenAccess W2090924127 @default.
- W2090924127 hasPrimaryLocation W20909241271 @default.
- W2090924127 hasRelatedWork W1578032312 @default.
- W2090924127 hasRelatedWork W1974686502 @default.
- W2090924127 hasRelatedWork W2001832527 @default.
- W2090924127 hasRelatedWork W2036177646 @default.
- W2090924127 hasRelatedWork W2053496175 @default.
- W2090924127 hasRelatedWork W2070678462 @default.
- W2090924127 hasRelatedWork W2237777144 @default.
- W2090924127 hasRelatedWork W4244366418 @default.
- W2090924127 hasRelatedWork W69397147 @default.
- W2090924127 hasRelatedWork W4300715300 @default.
- W2090924127 hasVolume "320" @default.
- W2090924127 isParatext "false" @default.
- W2090924127 isRetracted "false" @default.
- W2090924127 magId "2090924127" @default.
- W2090924127 workType "article" @default.