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http://purl.uniprot.org/citations/15910006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15910006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15910006http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15910006http://www.w3.org/2000/01/rdf-schema#comment"The human MOCS3 protein contains an N-terminal domain similar to the Escherichia coli MoeB protein and a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 is proposed to catalyze both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin (MPT) synthase during Moco biosynthesis in humans. Recent studies have shown that the MOCS3 rhodanese-like domain (MOCS3-RLD) catalyzes the transfer of sulfur from thiosulfate to cyanide and is also able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z. MOCS3-RLD contains four cysteine residues of which only C412 in the six amino acid active loop is conserved in homologous proteins from other organisms. ESI-MS/MS studies gave direct evidence for the formation of a persulfide group that is exclusively formed on C412. Simultaneous mutagenesis of the remaining three cysteine residues showed that none of them is involved in the sulfur transfer reaction in vitro. A disulfide bridge was identified to be formed between C316 and C324, and possible roles of the three noncatalytic cysteine residues are discussed. By ESI-MS/MS a partially gluconoylated N-terminus of the His6-tagged MOCS3-RLD was identified (mass increment of 178 Da) which resulted in a heterogeneity of the protein but did not influence sulfurtransferase activity."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.org/dc/terms/identifier"doi:10.1021/bi0503448"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.org/dc/terms/identifier"doi:10.1021/bi0503448"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Nimtz M."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Nimtz M."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Leimkuehler S."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Leimkuehler S."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Matthies A."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/author"Matthies A."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/pages"7912-7920"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/pages"7912-7920"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/title"Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/title"Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry."xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/15910006http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/15910006http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15910006
http://purl.uniprot.org/citations/15910006http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15910006
http://purl.uniprot.org/citations/15910006http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15910006