| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/2000/01/rdf-schema#comment | "Citrate lyase (EC 4.1.3.6) catalyzes the cleavage of citrate to acetate and oxaloacetate and is composed of three subunits (alpha, beta, and gamma). The gamma-subunit serves as an acyl carrier protein (ACP) and contains the prosthetic group 2'-(5' '-phosphoribosyl)-3'-dephospho-CoA, which is attached via a phosphodiester linkage to serine-14 in the enzyme from Klebsiella pneumoniae. In this work, we demonstrate by genetic and biochemical studies with citrate lyase of Escherichia coli and K. pneumoniae that the conversion of apo-ACP into holo-ACP is dependent on the two proteins, CitX (20 kDa) and CitG (33 kDa). In the absence of CitX, only apo-ACP was synthesized in vivo, whereas in the absence of CitG, an adenylylated ACP was produced, with the AMP residue attached to serine-14. The adenylyltransferase activity of CitX could be verified in vitro with purified CitX and apo-ACP plus ATP as substrates. Besides ATP, CTP, GTP, and UTP also served as nucleotidyl donors in vitro, showing that CitX functions as a nucleotidyltransferase. The conversion of apo-ACP into holo-ACP was achieved in vitro by incubation of apo-ACP with CitX, CitG, ATP, and dephospho-CoA. ATP could not be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-ACP was formed. Remarkably, it was not possible to further convert AMP-ACP to holo-ACP by subsequent incubation with CitG and dephospho-CoA. This demonstrates that AMP-ACP is not an intermediate during the conversion of apo-into holo-ACP, but results from a side activity of CitX that becomes effective in the absence of its natural substrate. Our results indicate that holo-ACP formation proceeds as follows. First, a prosthetic group precursor [presumably 2'-(5' '-triphosphoribosyl)-3'-dephospho-CoA] is formed from ATP and dephospho-CoA in a reaction catalyzed by CitG. Second, holo-ACP is formed from apo-ACP and the prosthetic group precursor in a reaction catalyzed by CitX."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi000401r"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi000401r"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi000401r"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Bott M."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Bott M."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Dimroth P."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Dimroth P."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Schneider K."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/author | "Schneider K."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/pages | "9438-9450"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/pages | "9438-9450"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/title | "Biosynthesis of the prosthetic group of citrate lyase."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/title | "Biosynthesis of the prosthetic group of citrate lyase."xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/volume | "39"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://purl.uniprot.org/core/volume | "39"xsd:string |
| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10924139 |
| http://purl.uniprot.org/citations/10924139 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10924139 |