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http://purl.uniprot.org/citations/15958387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15958387http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15958387http://www.w3.org/2000/01/rdf-schema#comment"AMID (apoptosis-inducing factor-homologous mitochondrion-associated inducer of death; also known as PRG3 (p53-responsive gene 3)) is a human caspase-independent pro-apoptotic protein with some similarity to apoptosis-inducing factor. AMID was purified from a recombinant bacterial host, enabling biochemical analysis of the protein. AMID is a flavoprotein; possesses NAD(P)H oxidase activity; and catalyzes NAD(P)H-dependent reduction of cytochrome c and other electron acceptors, including molecular oxygen. NADPH binds approximately 10-fold tighter than NADH. AMID binds 6-hydroxy-FAD (a cofactor that accumulates only adventitiously and at low abundance in other flavoprotein enzymes) to form a stoichiometric cofactor.protein complex. AMID has a distinctive electronic spectrum due to the modified flavin. NAD(P)+ binding perturbed the spectrum, enabling determination of K(d) values for these coenzymes. 6-Hydroxy-FAD could be removed from AMID and the apoprotein reconstituted with FAD. FAD was converted to 6-hydroxy-FAD in reconstituted AMID during aerobic turnover with NADPH. AMID is a DNA-binding protein that lacks apparent DNA sequence specificity. Formation of the protein.DNA complex (i) effected a major protein conformational change and (ii) was prevented in the presence of nicotinamide coenzyme. Apo-AMID retains DNA binding activity. Our studies establish a link between coenzyme and DNA binding that likely impacts on the physiological role of AMID in cellular apoptosis."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m414018200"xsd:string
http://purl.uniprot.org/citations/15958387http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m414018200"xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Munro A.W."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Munro A.W."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Gong M."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Gong M."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Scrutton N.S."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Scrutton N.S."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Marshall K.R."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Marshall K.R."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Farmer P.B."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Farmer P.B."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Jones D.J."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Jones D.J."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Lamb J.H."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Lamb J.H."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Wodke L."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/author"Wodke L."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15958387http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string