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http://purl.uniprot.org/citations/31964920http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31964920http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31964920http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/31964920http://www.w3.org/2000/01/rdf-schema#comment"Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid Escherichia coli protein YqfB, previously identified as hypothetical, is a unique ASCH domain-containing amidohydrolase responsible for the catabolism of N4-acetylcytidine (ac4C). YqfB has several interesting and unique features: i) it is the smallest monomeric amidohydrolase described to date, ii) it is active towards structurally different N4-acylated cytosines/cytidines, and iii) it has a high specificity for these substrates (kcat/Km up to 2.8 × 106 M-1 s-1). Moreover, our results suggest that YqfB contains a unique Thr-Lys-Glu catalytic triad, and Arg acting as an oxyanion hole. The mutant lacking the yqfB gene retains the ability to grow, albeit poorly, on N4-acetylcytosine as a source of uracil, suggesting that an alternative route for the utilization of this compound exists in E. coli. Overall, YqfB ability to hydrolyse various N4-acylated cytosines and cytidines not only sheds light on the long-standing mystery of how ac4C is catabolized in bacteria, but also expands our knowledge of the structural diversity within the active sites of amidohydrolases."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.org/dc/terms/identifier"doi:10.1038/s41598-020-57664-w"xsd:string
http://purl.uniprot.org/citations/31964920http://purl.org/dc/terms/identifier"doi:10.1038/s41598-020-57664-w"xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Aucynaite A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Aucynaite A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Kaliniene L."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Kaliniene L."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Kaupinis A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Kaupinis A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Laurynenas A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Laurynenas A."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Meskiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Meskiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Meskys R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Meskys R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Rutkiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Rutkiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Stanislauskiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Stanislauskiene R."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Tauraite D."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Tauraite D."xsd:string
http://purl.uniprot.org/citations/31964920http://purl.uniprot.org/core/author"Urbeliene N."xsd:string