| http://purl.uniprot.org/citations/9804851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9804851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9804851 | http://www.w3.org/2000/01/rdf-schema#comment | "The cyanide-resistant alternative oxidase of plant mitochondria is a homodimeric protein whose activity can be regulated by a redox-sensitive intersubunit sulfhydryl/disulfide system and by alpha-keto acids. After determining that the Arabidopsis alternative oxidase possesses the redox-sensitive sulfhydryl/disulfide system, site-directed mutagenesis of an Arabidopsis cDNA clone was used to individually change the two conserved Cys residues, Cys-128 and Cys-78, to Ala. Using diamide oxidation and chemical cross-linking of the protein expressed in Escherichia coli, Cys-78 was shown to be: 1) the Cys residue involved in the sulfhydryl/disulfide system; and 2) not required for subunit dimerization. The C128A mutant was stimulated by pyruvate, while the C78A mutant protein had little activity and displayed no stimulation by pyruvate. Mutating Cys-78 to Glu produced an active enzyme which was insensitive to pyruvate, consistent with alpha-keto acid activation occurring through a thiohemiacetal. These results indicate that Cys-78 serves as both the regulatory sulfhydryl/disulfide and the site of activation by alpha-keto acids. In light of these results, the previously observed effects of sulfhydryl reagents on the alternative oxidase of isolated soybean mitochondria were re-examined and were found to be in agreement with a single sulfhydryl residue being the site both of alpha-keto acid activation and of the regulatory sulfhydryl/disulfide system."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.46.30750"xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.273.46.30750"xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Sweet C.R."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Sweet C.R."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Lennon A.M."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Lennon A.M."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Rauch G.S."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Rauch G.S."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Rhoads D.M."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Rhoads D.M."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Siedow J.N."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Siedow J.N."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Umbach A.L."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/author | "Umbach A.L."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/pages | "30750-30756"xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/pages | "30750-30756"xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/title | "Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in alpha-keto acid stimulation and intersubunit disulfide bond formation."xsd:string |
| http://purl.uniprot.org/citations/9804851 | http://purl.uniprot.org/core/title | "Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in alpha-keto acid stimulation and intersubunit disulfide bond formation."xsd:string |