FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2047867213> ?p ?o ?g. }

• W2047867213 endingPage "24374" @default.
• W2047867213 startingPage "24370" @default.
• W2047867213 abstract "We describe a novel enzyme that hydrolyzes the N-acyl linkage between fatty acids and sphingosine bases in ceramides of various sphingolipids. The enzyme was purified about 300-fold with 5% recovery from the culture filtrate of a newly isolated bacterium (Pseudomonas sp. TK4) by ammonium sulfate precipitation followed by several steps of high performance liquid chromatography. The purified enzyme preparation was completely free of exoglycosidases, sphingomyelinase, and proteases, and showed a single protein band corresponding to a molecular mass of 52 kDa on SDS-polyacrylamide slab gel electrophoresis after staining with Coomassie Brilliant Blue. The enzyme shows quite wide specificity, i.e. it hydrolyzes both neutral and acidic glycosphingolipids, and simple glycosphingolipid cerebrosides to polysialogangliosides such as GQ1b. Furthermore the enzyme also hydrolyzes sphingomyelin to produce the respective lyso form. However, the enzyme shows hardly any activity on ceramides, indicating that it is completely different from the ceramidase (EC 3.5.1.23) reported previously. This enzyme, which is tentatively named sphingolipid ceramide N-deacylase, should greatly facilitate the further study of sphingolipids as well as lysosphingolipids. We describe a novel enzyme that hydrolyzes the N-acyl linkage between fatty acids and sphingosine bases in ceramides of various sphingolipids. The enzyme was purified about 300-fold with 5% recovery from the culture filtrate of a newly isolated bacterium (Pseudomonas sp. TK4) by ammonium sulfate precipitation followed by several steps of high performance liquid chromatography. The purified enzyme preparation was completely free of exoglycosidases, sphingomyelinase, and proteases, and showed a single protein band corresponding to a molecular mass of 52 kDa on SDS-polyacrylamide slab gel electrophoresis after staining with Coomassie Brilliant Blue. The enzyme shows quite wide specificity, i.e. it hydrolyzes both neutral and acidic glycosphingolipids, and simple glycosphingolipid cerebrosides to polysialogangliosides such as GQ1b. Furthermore the enzyme also hydrolyzes sphingomyelin to produce the respective lyso form. However, the enzyme shows hardly any activity on ceramides, indicating that it is completely different from the ceramidase (EC 3.5.1.23) reported previously. This enzyme, which is tentatively named sphingolipid ceramide N-deacylase, should greatly facilitate the further study of sphingolipids as well as lysosphingolipids." @default.
• W2047867213 created "2016-06-24" @default.
• W2047867213 creator A5039314894 @default.
• W2047867213 creator A5045942750 @default.
• W2047867213 creator A5050726856 @default.
• W2047867213 date "1995-10-01" @default.
• W2047867213 modified "2023-10-17" @default.
• W2047867213 title "A Novel Enzyme That Cleaves the N-Acyl Linkage of Ceramides in Various Glycosphingolipids as Well as Sphingomyelin to Produce Their Lyso Forms" @default.
• W2047867213 cites W1480588550 @default.
• W2047867213 cites W1555606052 @default.
• W2047867213 cites W1577542502 @default.
• W2047867213 cites W1594345523 @default.
• W2047867213 cites W1601227390 @default.
• W2047867213 cites W1611493774 @default.
• W2047867213 cites W181752127 @default.
• W2047867213 cites W1870526123 @default.
• W2047867213 cites W1981768734 @default.
• W2047867213 cites W2009373735 @default.
• W2047867213 cites W2026443244 @default.
• W2047867213 cites W2031855453 @default.
• W2047867213 cites W2056509744 @default.
• W2047867213 cites W2075836148 @default.
• W2047867213 cites W2081916366 @default.
• W2047867213 cites W2088359206 @default.
• W2047867213 cites W2094248354 @default.
• W2047867213 cites W2100837269 @default.
• W2047867213 cites W2104445534 @default.
• W2047867213 cites W2115262231 @default.
• W2047867213 cites W2146403600 @default.
• W2047867213 cites W2146646899 @default.
• W2047867213 cites W2151378459 @default.
• W2047867213 cites W2181816755 @default.
• W2047867213 cites W2212445342 @default.
• W2047867213 cites W2346329947 @default.
• W2047867213 cites W2409438283 @default.
• W2047867213 cites W38937041 @default.
• W2047867213 cites W4235428970 @default.
• W2047867213 doi "https://doi.org/10.1074/jbc.270.41.24370" @default.
• W2047867213 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7592649" @default.
• W2047867213 hasPublicationYear "1995" @default.
• W2047867213 type Work @default.
• W2047867213 sameAs 2047867213 @default.
• W2047867213 citedByCount "99" @default.
• W2047867213 countsByYear W20478672132012 @default.
• W2047867213 countsByYear W20478672132013 @default.
• W2047867213 countsByYear W20478672132014 @default.
• W2047867213 countsByYear W20478672132015 @default.
• W2047867213 countsByYear W20478672132016 @default.
• W2047867213 countsByYear W20478672132017 @default.
• W2047867213 countsByYear W20478672132018 @default.
• W2047867213 countsByYear W20478672132019 @default.
• W2047867213 countsByYear W20478672132021 @default.
• W2047867213 countsByYear W20478672132023 @default.
• W2047867213 crossrefType "journal-article" @default.
• W2047867213 hasAuthorship W2047867213A5039314894 @default.
• W2047867213 hasAuthorship W2047867213A5045942750 @default.
• W2047867213 hasAuthorship W2047867213A5050726856 @default.
• W2047867213 hasBestOaLocation W20478672131 @default.
• W2047867213 hasConcept C170493617 @default.
• W2047867213 hasConcept C181199279 @default.
• W2047867213 hasConcept C185592680 @default.
• W2047867213 hasConcept C190283241 @default.
• W2047867213 hasConcept C193363816 @default.
• W2047867213 hasConcept C2776428949 @default.
• W2047867213 hasConcept C2777851122 @default.
• W2047867213 hasConcept C2778139943 @default.
• W2047867213 hasConcept C2778197599 @default.
• W2047867213 hasConcept C2778703144 @default.
• W2047867213 hasConcept C2780120296 @default.
• W2047867213 hasConcept C41625074 @default.
• W2047867213 hasConcept C43617362 @default.
• W2047867213 hasConcept C55493867 @default.
• W2047867213 hasConcept C61322309 @default.
• W2047867213 hasConcept C61705674 @default.
• W2047867213 hasConceptScore W2047867213C170493617 @default.
• W2047867213 hasConceptScore W2047867213C181199279 @default.
• W2047867213 hasConceptScore W2047867213C185592680 @default.
• W2047867213 hasConceptScore W2047867213C190283241 @default.
• W2047867213 hasConceptScore W2047867213C193363816 @default.
• W2047867213 hasConceptScore W2047867213C2776428949 @default.
• W2047867213 hasConceptScore W2047867213C2777851122 @default.
• W2047867213 hasConceptScore W2047867213C2778139943 @default.
• W2047867213 hasConceptScore W2047867213C2778197599 @default.
• W2047867213 hasConceptScore W2047867213C2778703144 @default.
• W2047867213 hasConceptScore W2047867213C2780120296 @default.
• W2047867213 hasConceptScore W2047867213C41625074 @default.
• W2047867213 hasConceptScore W2047867213C43617362 @default.
• W2047867213 hasConceptScore W2047867213C55493867 @default.
• W2047867213 hasConceptScore W2047867213C61322309 @default.
• W2047867213 hasConceptScore W2047867213C61705674 @default.
• W2047867213 hasIssue "41" @default.
• W2047867213 hasLocation W20478672131 @default.
• W2047867213 hasOpenAccess W2047867213 @default.
• W2047867213 hasPrimaryLocation W20478672131 @default.
• W2047867213 hasRelatedWork W1567111656 @default.
• W2047867213 hasRelatedWork W1889741616 @default.
• W2047867213 hasRelatedWork W2014162410 @default.
• W2047867213 hasRelatedWork W2021690838 @default.

• next