Matches in SemOpenAlex for { <https://semopenalex.org/work/W2024256713> ?p ?o ?g. }
Showing items 1 to 74 of
74
with 100 items per page.
- W2024256713 endingPage "2737" @default.
- W2024256713 startingPage "2725" @default.
- W2024256713 abstract "An unusual flavoprotein disulfide reductase, which catalyzes the NADPH-dependent reduction of CoASSCoA, has recently been purified from the human pathogen Staphylococcus aureus [delCardayré, S. B., Stock, K. P., Newton, G. L., Fahey, R. C., and Davies, J. E. (1998) J. Biol. Chem. 273, 5744-5751]. Coenzyme A-disulfide reductase (CoADR) lacks the redox-active protein disulfide characteristic of the disulfide reductases; instead, NADPH reduction yields 1 protein-SH and 1 CoASH. Furthermore, the CoADR sequence reveals the presence of a single putative active-site Cys (Cys43) within an SFXXC motif also seen in the Enterococcus faecalis NADH oxidase and NADH peroxidase, which use a single redox-active cysteine-sulfenic acid in catalysis. In this report, we provide a detailed examination of the equilibrium properties of both wild-type and C43S CoADRs, focusing on the role of Cys43 in the catalytic redox cycle, the behavior of both enzyme forms on reduction with dithionite and NADPH, and the interaction of NADP+ with the corresponding reduced enzyme species. The results of these analyses, combined with electrospray mass spectrometric data for the two oxidized enzyme forms, fully support the catalytic redox role proposed for Cys43 and confirm that this is the attachment site for bound CoASH. In addition, we provide evidence indicating dramatic thermodynamic inequivalence between the two active sites per dimer, similar to that documented for the related enzymes mercuric reductase and NADH oxidase; only 1 FAD is reduced with NADPH in wild-type CoADR. The EH2.NADPH/EH4.NADP+ complex which results is reoxidized quantitatively in titrations with CoASSCoA, supporting a possible role for the asymmetric reduced dimer in catalysis." @default.
- W2024256713 created "2016-06-24" @default.
- W2024256713 creator A5030484863 @default.
- W2024256713 creator A5053682424 @default.
- W2024256713 creator A5088827548 @default.
- W2024256713 date "1999-02-09" @default.
- W2024256713 modified "2023-10-18" @default.
- W2024256713 title "Coenzyme A-Disulfide Reductase from <i>Staphylococcus aureus</i>: Evidence for Asymmetric Behavior on Interaction with Pyridine Nucleotides" @default.
- W2024256713 cites W1549181628 @default.
- W2024256713 cites W2129504476 @default.
- W2024256713 doi "https://doi.org/10.1021/bi9825899" @default.
- W2024256713 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10052943" @default.
- W2024256713 hasPublicationYear "1999" @default.
- W2024256713 type Work @default.
- W2024256713 sameAs 2024256713 @default.
- W2024256713 citedByCount "31" @default.
- W2024256713 countsByYear W20242567132012 @default.
- W2024256713 countsByYear W20242567132013 @default.
- W2024256713 countsByYear W20242567132014 @default.
- W2024256713 countsByYear W20242567132018 @default.
- W2024256713 countsByYear W20242567132019 @default.
- W2024256713 countsByYear W20242567132022 @default.
- W2024256713 crossrefType "journal-article" @default.
- W2024256713 hasAuthorship W2024256713A5030484863 @default.
- W2024256713 hasAuthorship W2024256713A5053682424 @default.
- W2024256713 hasAuthorship W2024256713A5088827548 @default.
- W2024256713 hasConcept C134651460 @default.
- W2024256713 hasConcept C178790620 @default.
- W2024256713 hasConcept C181199279 @default.
- W2024256713 hasConcept C185592680 @default.
- W2024256713 hasConcept C197957613 @default.
- W2024256713 hasConcept C2777315085 @default.
- W2024256713 hasConcept C2779201268 @default.
- W2024256713 hasConcept C33093398 @default.
- W2024256713 hasConcept C41183919 @default.
- W2024256713 hasConcept C55493867 @default.
- W2024256713 hasConcept C55904794 @default.
- W2024256713 hasConcept C71240020 @default.
- W2024256713 hasConcept C71995715 @default.
- W2024256713 hasConceptScore W2024256713C134651460 @default.
- W2024256713 hasConceptScore W2024256713C178790620 @default.
- W2024256713 hasConceptScore W2024256713C181199279 @default.
- W2024256713 hasConceptScore W2024256713C185592680 @default.
- W2024256713 hasConceptScore W2024256713C197957613 @default.
- W2024256713 hasConceptScore W2024256713C2777315085 @default.
- W2024256713 hasConceptScore W2024256713C2779201268 @default.
- W2024256713 hasConceptScore W2024256713C33093398 @default.
- W2024256713 hasConceptScore W2024256713C41183919 @default.
- W2024256713 hasConceptScore W2024256713C55493867 @default.
- W2024256713 hasConceptScore W2024256713C55904794 @default.
- W2024256713 hasConceptScore W2024256713C71240020 @default.
- W2024256713 hasConceptScore W2024256713C71995715 @default.
- W2024256713 hasIssue "9" @default.
- W2024256713 hasLocation W20242567131 @default.
- W2024256713 hasLocation W20242567132 @default.
- W2024256713 hasOpenAccess W2024256713 @default.
- W2024256713 hasPrimaryLocation W20242567131 @default.
- W2024256713 hasRelatedWork W1997428826 @default.
- W2024256713 hasRelatedWork W2003889801 @default.
- W2024256713 hasRelatedWork W2034876507 @default.
- W2024256713 hasRelatedWork W2043604835 @default.
- W2024256713 hasRelatedWork W2091146030 @default.
- W2024256713 hasRelatedWork W2162473589 @default.
- W2024256713 hasRelatedWork W2254626154 @default.
- W2024256713 hasRelatedWork W2336018257 @default.
- W2024256713 hasRelatedWork W2491465253 @default.
- W2024256713 hasRelatedWork W3137522507 @default.
- W2024256713 hasVolume "38" @default.
- W2024256713 isParatext "false" @default.
- W2024256713 isRetracted "false" @default.
- W2024256713 magId "2024256713" @default.
- W2024256713 workType "article" @default.