| http://purl.uniprot.org/citations/28045519 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28045519 | http://www.w3.org/2000/01/rdf-schema#comment | "Radical S-adenosyl-l-methionine (SAM) enzymes are widely distributed and catalyze diverse reactions. SAM binds to the unique iron atom of a site-differentiated [4Fe-4S] cluster and is reductively cleaved to generate a 5'-deoxyadenosyl radical, which initiates turnover. 7-Carboxy-7-deazaguanine (CDG) synthase (QueE) catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products. 6-Carboxypterin (6-CP), an oxidized analogue of the natural substrate 6-carboxy-5,6,7,8-tetrahydropterin (CPH4), is shown to be an alternate substrate for CDG synthase. Under reducing conditions that would promote the reductive cleavage of SAM, 6-CP is turned over to 6-deoxyadenosylpterin (6-dAP), presumably by radical addition of the 5'-deoxyadenosine followed by oxidative decarboxylation to the product. By contrast, in the absence of the strong reductant, dithionite, the carboxylate of 6-CP is esterified to generate 6-carboxypterin-5'-deoxyadenosyl ester (6-CP-dAdo ester). Structural studies with 6-CP and SAM also reveal electron density consistent with the ester product being formed in crystallo. The differential reactivity of 6-CP under reducing and nonreducing conditions highlights the ability of radical SAM enzymes to carry out both polar and radical transformations in the same active site."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.org/dc/terms/identifier | "doi:10.1021/jacs.6b11381"xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "Bandarian V."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "Dowling D.P."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "Drennan C.L."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "Bruender N.A."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "McCarty R.M."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/author | "Grell T.A."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/name | "J Am Chem Soc"xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/pages | "1912-1920"xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/title | "7-Carboxy-7-deazaguanine Synthase: A Radical S-Adenosyl-l-methionine Enzyme with Polar Tendencies."xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://purl.uniprot.org/core/volume | "139"xsd:string |
| http://purl.uniprot.org/citations/28045519 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28045519 |
| http://purl.uniprot.org/citations/28045519 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28045519 |
| http://purl.uniprot.org/uniprot/#_O31677-mappedCitation-28045519 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28045519 |
| http://purl.uniprot.org/uniprot/O31677 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/28045519 |