http://purl.uniprot.org/citations/27467699 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/27467699 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/27467699 | http://www.w3.org/2000/01/rdf-schema#comment | "All methanogenic and methanotrophic archaea known to date contain methyl-coenzyme M reductase (MCR) that catalyzes the reversible reduction of methyl-coenzyme M to methane. This enzyme contains the nickel porphinoid F430 as a prosthetic group and, highly conserved, a thioglycine and four methylated amino acid residues near the active site. We describe herein the presence of a novel post-translationally modified amino acid, didehydroaspartate, adjacent to the thioglycine as revealed by mass spectrometry and high-resolution X-ray crystallography. Upon chemical reduction, the didehydroaspartate residue was converted into aspartate. Didehydroaspartate was found in MCR I and II from Methanothermobacter marburgensis and in MCR of phylogenetically distantly related Methanosarcina barkeri but not in MCR I and II of Methanothermobacter wolfeii, which indicates that didehydroaspartate is dispensable but might have a role in fine-tuning the active site to increase the catalytic efficiency."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.org/dc/terms/identifier | "doi:10.1002/anie.201603882"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.org/dc/terms/identifier | "doi:10.1002/anie.201603882"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Ermler U."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Ermler U."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Kahnt J."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Kahnt J."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Shima S."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Shima S."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Wagner T."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/author | "Wagner T."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/name | "Angew. Chem. Int. Ed. Engl."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/name | "Angew. Chem. Int. Ed. Engl."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/pages | "10630-10633"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/pages | "10630-10633"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/title | "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing Methane Formation."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/title | "Didehydroaspartate Modification in Methyl-CoenzymeM Reductase Catalyzing Methane Formation."xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/volume | "55"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://purl.uniprot.org/core/volume | "55"xsd:string |
http://purl.uniprot.org/citations/27467699 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27467699 |
http://purl.uniprot.org/citations/27467699 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27467699 |