| http://purl.uniprot.org/citations/15561708 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15561708 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15561708 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15561708 | http://www.w3.org/2000/01/rdf-schema#comment | "The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana specifically regulates the activity of the molybdenum enzymes aldehyde oxidase and xanthine dehydrogenase by converting their molybdenum cofactor from the desulfo-form into the sulfo-form. ABA3 is a two-domain protein with an NH2-terminal domain sharing significant similarities to NifS proteins that catalyze the decomposition of l-cysteine to l-alanine and elemental sulfur for iron-sulfur cluster synthesis. Although different in its physiological function, the mechanism of ABA3 for sulfur mobilization was found to be similar to NifS proteins. The protein binds a pyridoxal phosphate cofactor and a substrate-derived persulfide intermediate, and site-directed mutagenesis of strictly conserved binding sites for the cofactor and the persulfide demonstrated that they are essential for molybdenum cofactor sulfurase activity. In vitro, the NifS-like domain of ABA3 activates aldehyde oxidase and xanthine dehydrogenase in the absence of the C-terminal domain, but in vivo, the C-terminal domain is required for proper activation of both target enzymes. In addition to its cysteine desulfurase activity, ABA3-NifS also exhibits selenocysteine lyase activity. Although l-selenocysteine is unlikely to be a natural substrate for ABA3, it is decomposed more efficiently than l-cysteine. Besides mitochondrial AtNFS1 and plastidial AtNFS2, which are both proposed to be involved in iron-sulfur cluster formation, ABA3 is proposed to be a third and cytosolic NifS-like cysteine desulfurase in A. thaliana. However, the sulfur transferase activity of ABA3 is used for post-translational activation of molybdenum enzymes rather than for iron-sulfur cluster assembly."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m411195200"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m411195200"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Bittner F."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Bittner F."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Mendel R.R."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Mendel R.R."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Heidenreich T."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Heidenreich T."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Wollers S."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/author | "Wollers S."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/pages | "4213-4218"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/pages | "4213-4218"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/title | "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/title | "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration."xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/15561708 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15561708 |