Matches in SemOpenAlex for { <https://semopenalex.org/work/W2014700836> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W2014700836 endingPage "8806" @default.
- W2014700836 startingPage "8798" @default.
- W2014700836 abstract "l-δ-(α-Aminoadipoyl)-l-cysteinyl-d-valine (ACV) synthetase is probably the simplest known peptide synthetase in terms of the number of reactions catalyzed. In the “thiol-template” proposal for nonribosomal peptide synthesis, a key step is transfer of aminoacyl groups derived from the substrates to enzyme-bound thiols prior to peptide bond formation. No incorporation of 18O was seen in AMP isolated from the reaction mixture when di[18O]valine was incubated with relatively large amounts of active synthetase and MgATP. We therefore utilized di[18O]valine as a substrate for the biosynthesis of the diastereomeric dipeptides l-O-(methylserinyl)-l-valine and l-O-(methylserinyl)-d-valine [Shiau, C.-Y., Baldwin, J. E., Byford, M. F., Sobey, W. J., & Schofield, C. J. (1995) FEBS Lett. 358, 97−100]. In the l-O-(methylserinyl)-l-valine product, no significant loss of 18O was observed. However, in the l-O-(methylserinyl)-d-valine product, a significant loss of one or both 18O labels was observed. Thus, both peptide bond formation and the epimerization of the valine residue can both occur before formation of any thioester bond to the valine carboxylate in the biosynthesis of these dipeptides. The usual qualitative test for thioesterification of substrates to the synthetase, lability of enzyme-bound radiolabeled amino acid to performic acid, proved inconclusive in our hands. These results require a new mechanism for the enzymic synthesis of l-O-(methylserinyl)-l-valine and l-O-(methylserinyl)-d-valine and imply that a revised mechanism for ACV synthesis is also required." @default.
- W2014700836 created "2016-06-24" @default.
- W2014700836 creator A5007267276 @default.
- W2014700836 creator A5013687869 @default.
- W2014700836 creator A5042398293 @default.
- W2014700836 creator A5088578643 @default.
- W2014700836 creator A5090281591 @default.
- W2014700836 date "1997-07-01" @default.
- W2014700836 modified "2023-09-25" @default.
- W2014700836 title "l-δ-(α-Aminoadipoyl)-l-cysteinyl-d-valine Synthetase: Thioesterification of Valine Is Not Obligatory for Peptide Bond Formation†" @default.
- W2014700836 cites W1553363451 @default.
- W2014700836 cites W1561140704 @default.
- W2014700836 cites W1580129210 @default.
- W2014700836 cites W1582513609 @default.
- W2014700836 cites W1983460849 @default.
- W2014700836 cites W1996610802 @default.
- W2014700836 cites W2011915862 @default.
- W2014700836 cites W2018558910 @default.
- W2014700836 cites W2062867967 @default.
- W2014700836 cites W2083843153 @default.
- W2014700836 cites W2089475202 @default.
- W2014700836 cites W2396152623 @default.
- W2014700836 cites W2419166996 @default.
- W2014700836 doi "https://doi.org/10.1021/bi962932e" @default.
- W2014700836 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9220966" @default.
- W2014700836 hasPublicationYear "1997" @default.
- W2014700836 type Work @default.
- W2014700836 sameAs 2014700836 @default.
- W2014700836 citedByCount "14" @default.
- W2014700836 countsByYear W20147008362013 @default.
- W2014700836 countsByYear W20147008362017 @default.
- W2014700836 crossrefType "journal-article" @default.
- W2014700836 hasAuthorship W2014700836A5007267276 @default.
- W2014700836 hasAuthorship W2014700836A5013687869 @default.
- W2014700836 hasAuthorship W2014700836A5042398293 @default.
- W2014700836 hasAuthorship W2014700836A5088578643 @default.
- W2014700836 hasAuthorship W2014700836A5090281591 @default.
- W2014700836 hasConcept C181199279 @default.
- W2014700836 hasConcept C185592680 @default.
- W2014700836 hasConcept C2777573094 @default.
- W2014700836 hasConcept C2778834346 @default.
- W2014700836 hasConcept C2779281246 @default.
- W2014700836 hasConcept C31684184 @default.
- W2014700836 hasConcept C515207424 @default.
- W2014700836 hasConcept C553450214 @default.
- W2014700836 hasConcept C55493867 @default.
- W2014700836 hasConcept C71240020 @default.
- W2014700836 hasConceptScore W2014700836C181199279 @default.
- W2014700836 hasConceptScore W2014700836C185592680 @default.
- W2014700836 hasConceptScore W2014700836C2777573094 @default.
- W2014700836 hasConceptScore W2014700836C2778834346 @default.
- W2014700836 hasConceptScore W2014700836C2779281246 @default.
- W2014700836 hasConceptScore W2014700836C31684184 @default.
- W2014700836 hasConceptScore W2014700836C515207424 @default.
- W2014700836 hasConceptScore W2014700836C553450214 @default.
- W2014700836 hasConceptScore W2014700836C55493867 @default.
- W2014700836 hasConceptScore W2014700836C71240020 @default.
- W2014700836 hasIssue "29" @default.
- W2014700836 hasLocation W20147008361 @default.
- W2014700836 hasLocation W20147008362 @default.
- W2014700836 hasOpenAccess W2014700836 @default.
- W2014700836 hasPrimaryLocation W20147008361 @default.
- W2014700836 hasRelatedWork W1816636001 @default.
- W2014700836 hasRelatedWork W1867182534 @default.
- W2014700836 hasRelatedWork W195232043 @default.
- W2014700836 hasRelatedWork W1996187565 @default.
- W2014700836 hasRelatedWork W2093059412 @default.
- W2014700836 hasRelatedWork W2156847831 @default.
- W2014700836 hasRelatedWork W2161246113 @default.
- W2014700836 hasRelatedWork W2409612133 @default.
- W2014700836 hasRelatedWork W3131068657 @default.
- W2014700836 hasRelatedWork W4283830725 @default.
- W2014700836 hasVolume "36" @default.
- W2014700836 isParatext "false" @default.
- W2014700836 isRetracted "false" @default.
- W2014700836 magId "2014700836" @default.
- W2014700836 workType "article" @default.