FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000383385> ?p ?o ?g. }

• W2000383385 endingPage "1367" @default.
• W2000383385 startingPage "1360" @default.
• W2000383385 abstract "ABSTRACT The acyl coenzyme A (acyl-CoA) dehydrogenases (ACADs) FadE34 and CasC, encoded by the cholesterol and cholate gene clusters of Mycobacterium tuberculosis and Rhodococcus jostii RHA1, respectively, were successfully purified. Both enzymes differ from previously characterized ACADs in that they contain two fused acyl-CoA dehydrogenase domains in a single polypeptide. Site-specific mutagenesis showed that only the C-terminal ACAD domain contains the catalytic glutamate base required for enzyme activity, while the N-terminal ACAD domain contains an arginine required for ionic interactions with the pyrophosphate of the flavin adenine dinucleotide (FAD) cofactor. Therefore, the two ACAD domains must associate to form a single active site. FadE34 and CasC were not active toward the 3-carbon side chain steroid metabolite 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA (4BNC-CoA) but were active toward steroid CoA esters containing 5-carbon side chains. CasC has similar specificity constants for cholyl-CoA, deoxycholyl-CoA, and 3β-hydroxy-5-cholen-24-oyl-CoA, while FadE34 has a preference for the last compound, which has a ring structure similar to that of cholesterol metabolites. Knockout of the casC gene in R. jostii RHA1 resulted in a reduced growth on cholate as a sole carbon source and accumulation of a 5-carbon side chain cholate metabolite. FadE34 and CasC represent unique members of ACADs with primary structures and substrate specificities that are distinct from those of previously characterized ACADs. IMPORTANCE We report here the identification and characterization of acyl-CoA dehydrogenases (ACADs) involved in the metabolism of 5-carbon side chains of cholesterol and cholate. The two homologous enzymes FadE34 and CasC, from M. tuberculosis and Rhodococcus jostii RHA1, respectively, contain two ACAD domains per polypeptide, and we show that these two domains interact to form a single active site. FadE34 and CasC are therefore representatives of a new class of ACADs with unique primary and quaternary structures. The bacterial steroid degradation pathway is important for the removal of steroid waste in the environment and for survival of the pathogen M. tuberculosis within host macrophages. FadE34 is a potential target for development of new antibiotics against tuberculosis." @default.
• W2000383385 created "2016-06-24" @default.
• W2000383385 creator A5008380449 @default.
• W2000383385 creator A5011192029 @default.
• W2000383385 creator A5028571482 @default.
• W2000383385 creator A5072711679 @default.
• W2000383385 creator A5079467486 @default.
• W2000383385 date "2015-04-15" @default.
• W2000383385 modified "2023-09-25" @default.
• W2000383385 title "Characterization of Novel Acyl Coenzyme A Dehydrogenases Involved in Bacterial Steroid Degradation" @default.
• W2000383385 cites W1577082055 @default.
• W2000383385 cites W1839665474 @default.
• W2000383385 cites W1972251269 @default.
• W2000383385 cites W1980340481 @default.
• W2000383385 cites W1984623258 @default.
• W2000383385 cites W2004270960 @default.
• W2000383385 cites W2005974395 @default.
• W2000383385 cites W2008691119 @default.
• W2000383385 cites W2012000929 @default.
• W2000383385 cites W2017231250 @default.
• W2000383385 cites W2017515789 @default.
• W2000383385 cites W2026710113 @default.
• W2000383385 cites W2030632688 @default.
• W2000383385 cites W2038529067 @default.
• W2000383385 cites W2047510552 @default.
• W2000383385 cites W2062412316 @default.
• W2000383385 cites W2067576392 @default.
• W2000383385 cites W2082315404 @default.
• W2000383385 cites W2086780915 @default.
• W2000383385 cites W2093363647 @default.
• W2000383385 cites W2106515170 @default.
• W2000383385 cites W2107644675 @default.
• W2000383385 cites W2109749350 @default.
• W2000383385 cites W2112759250 @default.
• W2000383385 cites W2128635872 @default.
• W2000383385 cites W2137015675 @default.
• W2000383385 cites W2138324725 @default.
• W2000383385 cites W2140354550 @default.
• W2000383385 cites W2155612026 @default.
• W2000383385 cites W2162347177 @default.
• W2000383385 cites W2162362966 @default.
• W2000383385 cites W2163297627 @default.
• W2000383385 cites W2189955651 @default.
• W2000383385 cites W2397911901 @default.
• W2000383385 cites W4293247451 @default.
• W2000383385 doi "https://doi.org/10.1128/jb.02420-14" @default.
• W2000383385 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4372733" @default.
• W2000383385 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25645564" @default.
• W2000383385 hasPublicationYear "2015" @default.
• W2000383385 type Work @default.
• W2000383385 sameAs 2000383385 @default.
• W2000383385 citedByCount "21" @default.
• W2000383385 countsByYear W20003833852016 @default.
• W2000383385 countsByYear W20003833852017 @default.
• W2000383385 countsByYear W20003833852018 @default.
• W2000383385 countsByYear W20003833852019 @default.
• W2000383385 countsByYear W20003833852020 @default.
• W2000383385 countsByYear W20003833852021 @default.
• W2000383385 countsByYear W20003833852022 @default.
• W2000383385 crossrefType "journal-article" @default.
• W2000383385 hasAuthorship W2000383385A5008380449 @default.
• W2000383385 hasAuthorship W2000383385A5011192029 @default.
• W2000383385 hasAuthorship W2000383385A5028571482 @default.
• W2000383385 hasAuthorship W2000383385A5072711679 @default.
• W2000383385 hasAuthorship W2000383385A5079467486 @default.
• W2000383385 hasBestOaLocation W20003833851 @default.
• W2000383385 hasConcept C134651460 @default.
• W2000383385 hasConcept C181199279 @default.
• W2000383385 hasConcept C185592680 @default.
• W2000383385 hasConcept C197957613 @default.
• W2000383385 hasConcept C2775859393 @default.
• W2000383385 hasConcept C2776317432 @default.
• W2000383385 hasConcept C2777477808 @default.
• W2000383385 hasConcept C2779123261 @default.
• W2000383385 hasConcept C2779387492 @default.
• W2000383385 hasConcept C2780902042 @default.
• W2000383385 hasConcept C55493867 @default.
• W2000383385 hasConcept C71240020 @default.
• W2000383385 hasConcept C71315377 @default.
• W2000383385 hasConcept C86803240 @default.
• W2000383385 hasConceptScore W2000383385C134651460 @default.
• W2000383385 hasConceptScore W2000383385C181199279 @default.
• W2000383385 hasConceptScore W2000383385C185592680 @default.
• W2000383385 hasConceptScore W2000383385C197957613 @default.
• W2000383385 hasConceptScore W2000383385C2775859393 @default.
• W2000383385 hasConceptScore W2000383385C2776317432 @default.
• W2000383385 hasConceptScore W2000383385C2777477808 @default.
• W2000383385 hasConceptScore W2000383385C2779123261 @default.
• W2000383385 hasConceptScore W2000383385C2779387492 @default.
• W2000383385 hasConceptScore W2000383385C2780902042 @default.
• W2000383385 hasConceptScore W2000383385C55493867 @default.
• W2000383385 hasConceptScore W2000383385C71240020 @default.
• W2000383385 hasConceptScore W2000383385C71315377 @default.
• W2000383385 hasConceptScore W2000383385C86803240 @default.
• W2000383385 hasIssue "8" @default.
• W2000383385 hasLocation W20003833851 @default.
• W2000383385 hasLocation W20003833852 @default.
• W2000383385 hasLocation W20003833853 @default.

• next