FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1504606556> ?p ?o ?g. }

• W1504606556 endingPage "4744" @default.
• W1504606556 startingPage "4732" @default.
• W1504606556 abstract "Abstract The fatty acid synthetase complex of pigeon liver has been dissociated (greater than 95%) into half-molecular weight subunits by dialyzing against Tris-glycine buffer, pH 8.3, containing 1 mm 2-mercaptoethanol or 1 mm dithiothreitol. The dissociated enzyme has very little activity for the synthesis of palmitic acid. However, it can be reassociated by dialysis against 0.2 m potassium phosphate, pH 7.0, containing 10 mm dithiothreitol. The reassociated enzyme has the same sedimentation coefficient and the same specific activity for fatty acid synthesis as the untreated complex. Comparisons have been made between the complex and the mixture of subunits for each of the partial reactions of fatty acid synthesis. Acetyl- and malonyl-CoA-pantetheine transacylase activities are, respectively, 30 and 50% lower in the dissociated enzyme than in the complex. The Km(app) values for the complex and the subunits are quite similar for the reduction of S-acetoacetyl-N-acetyl cysteamine, dehydration of β-hydroxybutyryl-N-acetyl cysteamine, and the deacylation of palmityl-CoA. The Vmax values for these three reactions are also either identical for both enzyme species or approximately 30% lower for the dissociated units. The Vmax/Km(app) value for the reduction of crotonyl-N-acetyl cysteamine by the subunits is at least 50% of the value obtained with undissociated enzyme. The most significant difference between the two enzyme species is the absence of the condensation-CO2 exchange reaction (between malonyl-CoA, caproyl-CoA (hexanoyl-CoA), coenzyme-A, and NaH14CO3) in the dissociated enzyme. The transfer of acetyl and malonyl groups (from their CoA esters) to the different sites on the complex and dissociated enzyme has also been compared. The covalent binding of acetyl groups to the cysteine-SH site, which is essential for the condensation reaction, is eliminated in the dissociated enzyme, whereas the extent of transfer to the hydroxyl and the 4'-phosphopantetheine-SH sites is either unchanged or is enhanced. The covalent binding of malonyl groups to the hydroxyl of the dissociated enzyme is unaffected, whereas transfer to the 4'-phosphopantetheine is appreciably reduced. The dissociation process does not appear to have drastically altered the spatial arrangement around the active site of all of the component enzymes except those associated with the transfer of the acetyl group to the cysteine-SH site, and possibly those involved in the condensation-CO2 exchange reaction." @default.
• W1504606556 created "2016-06-24" @default.
• W1504606556 creator A5017506642 @default.
• W1504606556 creator A5029045950 @default.
• W1504606556 creator A5036769436 @default.
• W1504606556 creator A5069421954 @default.
• W1504606556 date "1970-09-01" @default.
• W1504606556 modified "2023-09-30" @default.
• W1504606556 title "Comparative Studies of the Pigeon Liver Fatty Acid Synthetase Complex and Its Subunits" @default.
• W1504606556 cites W104696514 @default.
• W1504606556 cites W134503978 @default.
• W1504606556 cites W1482999216 @default.
• W1504606556 cites W1506043065 @default.
• W1504606556 cites W1526291384 @default.
• W1504606556 cites W1532171941 @default.
• W1504606556 cites W1557690614 @default.
• W1504606556 cites W1594834988 @default.
• W1504606556 cites W1775143899 @default.
• W1504606556 cites W1965351776 @default.
• W1504606556 cites W1967383104 @default.
• W1504606556 cites W1970658076 @default.
• W1504606556 cites W1976037009 @default.
• W1504606556 cites W2006188156 @default.
• W1504606556 cites W2009731386 @default.
• W1504606556 cites W2014230245 @default.
• W1504606556 cites W2040799835 @default.
• W1504606556 cites W2042469368 @default.
• W1504606556 cites W2054662884 @default.
• W1504606556 cites W2067358905 @default.
• W1504606556 cites W2068515092 @default.
• W1504606556 cites W2078759138 @default.
• W1504606556 cites W2096873528 @default.
• W1504606556 cites W2165953224 @default.
• W1504606556 cites W2197966293 @default.
• W1504606556 cites W2316615221 @default.
• W1504606556 cites W2319629175 @default.
• W1504606556 cites W2320934986 @default.
• W1504606556 cites W2415121648 @default.
• W1504606556 cites W3026590205 @default.
• W1504606556 cites W48316491 @default.
• W1504606556 cites W80538366 @default.
• W1504606556 doi "https://doi.org/10.1016/s0021-9258(18)62855-8" @default.
• W1504606556 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5456146" @default.
• W1504606556 hasPublicationYear "1970" @default.
• W1504606556 type Work @default.
• W1504606556 sameAs 1504606556 @default.
• W1504606556 citedByCount "137" @default.
• W1504606556 countsByYear W15046065562012 @default.
• W1504606556 countsByYear W15046065562013 @default.
• W1504606556 countsByYear W15046065562015 @default.
• W1504606556 countsByYear W15046065562016 @default.
• W1504606556 countsByYear W15046065562021 @default.
• W1504606556 crossrefType "journal-article" @default.
• W1504606556 hasAuthorship W1504606556A5017506642 @default.
• W1504606556 hasAuthorship W1504606556A5029045950 @default.
• W1504606556 hasAuthorship W1504606556A5036769436 @default.
• W1504606556 hasAuthorship W1504606556A5069421954 @default.
• W1504606556 hasBestOaLocation W15046065561 @default.
• W1504606556 hasConcept C126322002 @default.
• W1504606556 hasConcept C185592680 @default.
• W1504606556 hasConcept C2778772119 @default.
• W1504606556 hasConcept C2779134260 @default.
• W1504606556 hasConcept C543025807 @default.
• W1504606556 hasConcept C55493867 @default.
• W1504606556 hasConcept C71924100 @default.
• W1504606556 hasConcept C86803240 @default.
• W1504606556 hasConceptScore W1504606556C126322002 @default.
• W1504606556 hasConceptScore W1504606556C185592680 @default.
• W1504606556 hasConceptScore W1504606556C2778772119 @default.
• W1504606556 hasConceptScore W1504606556C2779134260 @default.
• W1504606556 hasConceptScore W1504606556C543025807 @default.
• W1504606556 hasConceptScore W1504606556C55493867 @default.
• W1504606556 hasConceptScore W1504606556C71924100 @default.
• W1504606556 hasConceptScore W1504606556C86803240 @default.
• W1504606556 hasIssue "18" @default.
• W1504606556 hasLocation W15046065561 @default.
• W1504606556 hasOpenAccess W1504606556 @default.
• W1504606556 hasPrimaryLocation W15046065561 @default.
• W1504606556 hasRelatedWork W1532864556 @default.
• W1504606556 hasRelatedWork W1951304285 @default.
• W1504606556 hasRelatedWork W1961263733 @default.
• W1504606556 hasRelatedWork W1966155319 @default.
• W1504606556 hasRelatedWork W2045173278 @default.
• W1504606556 hasRelatedWork W2082877035 @default.
• W1504606556 hasRelatedWork W2372301901 @default.
• W1504606556 hasRelatedWork W2412965522 @default.
• W1504606556 hasRelatedWork W940379662 @default.
• W1504606556 hasRelatedWork W2189310716 @default.
• W1504606556 hasVolume "245" @default.
• W1504606556 isParatext "false" @default.
• W1504606556 isRetracted "false" @default.
• W1504606556 magId "1504606556" @default.
• W1504606556 workType "article" @default.