RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/7559576http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7559576http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7559576http://www.w3.org/2000/01/rdf-schema#comment"Holo-acyl carrier protein synthase (ACPS) transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to Ser-36 of acyl carrier protein (ACP) in Escherichia coli. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. We have purified E. coli ACPS to near homogeneity by exploiting the ability to refold ACPS and reconstitute its activity after elution from an apo-ACP affinity column under denaturing conditions. N-terminal sequencing of ACPS allowed us to identify dpj, an essential gene of previously unknown function, as the structural gene for ACPS. We report herein the 70,000-fold purification of wild-type ACPS and the overproduction and initial characterization of recombinant ACPS from E. coli."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.42.24658"xsd:string
http://purl.uniprot.org/citations/7559576http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.42.24658"xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/author"Walsh C.T."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/author"Walsh C.T."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/author"Lambalot R.H."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/author"Lambalot R.H."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/pages"24658-24661"xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/pages"24658-24661"xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/title"Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/title"Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase."xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7559576http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7559576http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7559576
http://purl.uniprot.org/citations/7559576http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7559576
http://purl.uniprot.org/citations/7559576http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7559576
http://purl.uniprot.org/citations/7559576http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7559576
http://purl.uniprot.org/uniprot/A0A8B6X986http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7559576
http://purl.uniprot.org/uniprot/P24224http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7559576