| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/2000/01/rdf-schema#comment | "Ribosomally synthesized post-translationally modified peptides (RiPPs) are encoded in the genomes of a wide variety of microorganisms, in the proximity of open reading frames that encode enzymes that conduct extensive modifications, many of which are novel. Recently, members of the radical S-adenosyl-l-methionine (SAM) superfamily have been identified in these biosynthetic clusters. Herein, we demonstrate the putative radical SAM enzyme, MftC, oxidatively decarboxylates the C-terminus of the MftA peptide in the presence of the accessory protein MftB. The reaction catalyzed by MftC expands the repertoire of peptide-based radical SAM chemistry beyond the intramolecular cross-links."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.biochem.6b00355"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.org/dc/terms/identifier | "doi:10.1021/acs.biochem.6b00355"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/author | "Bandarian V."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/author | "Bandarian V."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/author | "Bruender N.A."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/author | "Bruender N.A."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/pages | "2813-2816"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/pages | "2813-2816"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/title | "The Radical S-Adenosyl-L-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/title | "The Radical S-Adenosyl-L-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide."xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/volume | "55"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://purl.uniprot.org/core/volume | "55"xsd:string |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27158836 |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27158836 |
| http://purl.uniprot.org/citations/27158836 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27158836 |
| http://purl.uniprot.org/citations/27158836 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27158836 |
| http://purl.uniprot.org/citations/27158836 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27158836 |