FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2070436071> ?p ?o ?g. }

• W2070436071 endingPage "14116" @default.
• W2070436071 startingPage "14100" @default.
• W2070436071 abstract "In the PLP-requiring α2β2 tryptophan synthase complex, recognition of the substrate l-Ser at the β-site includes a loop structure (residues β110−115) extensively H-bonded to the substrate α-carboxylate. To investigate the relationship of this subsite to catalytic function and to the regulation of substrate channeling, two loop mutants were constructed: βThr110 → Val, and βGln114 → Asn. The βT110V mutation greatly impairs both catalytic activity in the β-reaction, and allosteric communication between the α- and β-sites. The crystal structure of the βT110V mutant shows that the modified l-Ser carboxylate subsite has altered protein interactions that impair β-site catalysis and the communication of allosteric signals between the α- and β-sites. Purified βQ114N consists of two species of mutant protein, one with a reddish color (λmax = 506 nm). The reddish species is unable to react with l-Ser. The second βQ114N species displays significant catalytic activities; however, intermediates obtained on reaction with substrate l-Ser and substrate analogues exhibit perturbed UV/vis absorption spectra. Incubation with l-Ser results in the formation of an inactive species during the first 15 min with λmax ∼ 320 nm, followed by a slower conversion over 24 h to the species with λmax = 506 nm. The 320 and 506 nm species originate from conversion of the α-aminoacrylate external aldimine to the internal aldimine and α-aminoacrylate, followed by the nucleophilic attack of α-aminoacrylate on C-4‘ of the internal aldimine to give a covalent adduct with PLP. Subsequent treatment with sodium hydroxide releases a modified coenzyme consisting of a vinylglyoxylic acid moiety linked through C-4‘ to the 4-position of the pyridine ring. We conclude that the shortening of the side chain accompanying the replacement of β114-Gln by Asn relaxes the steric constraints that prevent this reaction in the wild-type enzyme. This study reveals a new layer of structure−function interactions essential for reaction specificity in tryptophan synthase." @default.
• W2070436071 created "2016-06-24" @default.
• W2070436071 creator A5017980134 @default.
• W2070436071 creator A5045764880 @default.
• W2070436071 creator A5049787932 @default.
• W2070436071 creator A5055790348 @default.
• W2070436071 creator A5066630519 @default.
• W2070436071 creator A5074480362 @default.
• W2070436071 creator A5085832228 @default.
• W2070436071 date "2007-11-16" @default.
• W2070436071 modified "2023-09-30" @default.
• W2070436071 title "βQ114N and βT110V Mutations Reveal a Critically Important Role of the Substrate α-Carboxylate Site in the Reaction Specificity of Tryptophan Synthase" @default.
• W2070436071 cites W1510741444 @default.
• W2070436071 cites W1602279263 @default.
• W2070436071 cites W1981116229 @default.
• W2070436071 cites W1995017064 @default.
• W2070436071 cites W1999684566 @default.
• W2070436071 cites W2000840258 @default.
• W2070436071 cites W2022950330 @default.
• W2070436071 cites W2033832729 @default.
• W2070436071 cites W2074824070 @default.
• W2070436071 cites W2076831384 @default.
• W2070436071 cites W2127702556 @default.
• W2070436071 cites W2131942711 @default.
• W2070436071 cites W2135839939 @default.
• W2070436071 cites W2950462341 @default.
• W2070436071 doi "https://doi.org/10.1021/bi7008568" @default.
• W2070436071 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18004874" @default.
• W2070436071 hasPublicationYear "2007" @default.
• W2070436071 type Work @default.
• W2070436071 sameAs 2070436071 @default.
• W2070436071 citedByCount "23" @default.
• W2070436071 countsByYear W20704360712013 @default.
• W2070436071 countsByYear W20704360712015 @default.
• W2070436071 countsByYear W20704360712016 @default.
• W2070436071 countsByYear W20704360712017 @default.
• W2070436071 countsByYear W20704360712019 @default.
• W2070436071 countsByYear W20704360712020 @default.
• W2070436071 countsByYear W20704360712021 @default.
• W2070436071 countsByYear W20704360712022 @default.
• W2070436071 countsByYear W20704360712023 @default.
• W2070436071 crossrefType "journal-article" @default.
• W2070436071 hasAuthorship W2070436071A5017980134 @default.
• W2070436071 hasAuthorship W2070436071A5045764880 @default.
• W2070436071 hasAuthorship W2070436071A5049787932 @default.
• W2070436071 hasAuthorship W2070436071A5055790348 @default.
• W2070436071 hasAuthorship W2070436071A5066630519 @default.
• W2070436071 hasAuthorship W2070436071A5074480362 @default.
• W2070436071 hasAuthorship W2070436071A5085832228 @default.
• W2070436071 hasConcept C161790260 @default.
• W2070436071 hasConcept C166342909 @default.
• W2070436071 hasConcept C181199279 @default.
• W2070436071 hasConcept C185592680 @default.
• W2070436071 hasConcept C18903297 @default.
• W2070436071 hasConcept C197957613 @default.
• W2070436071 hasConcept C2776568683 @default.
• W2070436071 hasConcept C2777289219 @default.
• W2070436071 hasConcept C2778074193 @default.
• W2070436071 hasConcept C41183919 @default.
• W2070436071 hasConcept C55493867 @default.
• W2070436071 hasConcept C67524406 @default.
• W2070436071 hasConcept C71240020 @default.
• W2070436071 hasConcept C86803240 @default.
• W2070436071 hasConceptScore W2070436071C161790260 @default.
• W2070436071 hasConceptScore W2070436071C166342909 @default.
• W2070436071 hasConceptScore W2070436071C181199279 @default.
• W2070436071 hasConceptScore W2070436071C185592680 @default.
• W2070436071 hasConceptScore W2070436071C18903297 @default.
• W2070436071 hasConceptScore W2070436071C197957613 @default.
• W2070436071 hasConceptScore W2070436071C2776568683 @default.
• W2070436071 hasConceptScore W2070436071C2777289219 @default.
• W2070436071 hasConceptScore W2070436071C2778074193 @default.
• W2070436071 hasConceptScore W2070436071C41183919 @default.
• W2070436071 hasConceptScore W2070436071C55493867 @default.
• W2070436071 hasConceptScore W2070436071C67524406 @default.
• W2070436071 hasConceptScore W2070436071C71240020 @default.
• W2070436071 hasConceptScore W2070436071C86803240 @default.
• W2070436071 hasIssue "49" @default.
• W2070436071 hasLocation W20704360711 @default.
• W2070436071 hasLocation W20704360712 @default.
• W2070436071 hasOpenAccess W2070436071 @default.
• W2070436071 hasPrimaryLocation W20704360711 @default.
• W2070436071 hasRelatedWork W1978667110 @default.
• W2070436071 hasRelatedWork W1992459676 @default.
• W2070436071 hasRelatedWork W1995545479 @default.
• W2070436071 hasRelatedWork W2007232769 @default.
• W2070436071 hasRelatedWork W2044062294 @default.
• W2070436071 hasRelatedWork W2058374135 @default.
• W2070436071 hasRelatedWork W2076105148 @default.
• W2070436071 hasRelatedWork W2898911472 @default.
• W2070436071 hasRelatedWork W3165656843 @default.
• W2070436071 hasRelatedWork W3207545950 @default.
• W2070436071 hasVolume "46" @default.
• W2070436071 isParatext "false" @default.
• W2070436071 isRetracted "false" @default.
• W2070436071 magId "2070436071" @default.
• W2070436071 workType "article" @default.