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http://purl.uniprot.org/unirules/MF_00664#construct-template-68http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_00664#construct-var-4
http://purl.uniprot.org/unirules/MF_00664#construct-template-68http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_00664#construct-template-68http://spinrdf.org/sp#object"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain."xsd:string
http://purl.uniprot.org/unirules/MF_00664#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_00664#construct-template-68
http://purl.uniprot.org/unirules/MF_00664#construct-template-list-68http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_00664#construct-template-68