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@ARTICLE{Schneider:26938,
      author       = {Schneider, K. and Dimroth, B. M. and Bott, M.},
      title        = {{B}iosynthesis of the prosthetic group of citrate lyase},
      journal      = {Biochemistry},
      volume       = {39},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-26938},
      pages        = {9438 - 9450},
      year         = {2000},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Acyl Carrier Protein: biosynthesis / Amino Acid Sequence /
                      Apoproteins: biosynthesis / Carbon-Sulfur Ligases:
                      biosynthesis / Carbon-Sulfur Ligases: genetics / Coenzyme A:
                      biosynthesis / Enzyme Precursors: metabolism / Escherichia
                      coli: enzymology / Escherichia coli: genetics / Genes,
                      Bacterial / Molecular Sequence Data / Multienzyme Complexes:
                      biosynthesis / Multienzyme Complexes: chemistry /
                      Multienzyme Complexes: genetics / Multigene Family / Operon
                      / Oxo-Acid-Lyases: biosynthesis / Oxo-Acid-Lyases: chemistry
                      / Oxo-Acid-Lyases: genetics / Structure-Activity
                      Relationship / Acyl Carrier Protein (NLM Chemicals) /
                      Apoproteins (NLM Chemicals) / Enzyme Precursors (NLM
                      Chemicals) / Multienzyme Complexes (NLM Chemicals) /
                      dephosphocoenzyme A (NLM Chemicals) / Coenzyme A (NLM
                      Chemicals) / Oxo-Acid-Lyases (NLM Chemicals) / citrate
                      (pro-3S)-lyase (NLM Chemicals) / Carbon-Sulfur Ligases (NLM
                      Chemicals) / long-chain-fatty-acid-(acyl-carrier-protein)
                      ligase (NLM Chemicals) / citrate (pro-3S)-lyase ligase (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBT},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB184},
      pnm          = {Entwicklung von Mikroorganismen für die Herstellung von
                      Primärmetaboliten},
      pid          = {G:(DE-Juel1)FUEK91},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:10924139},
      UT           = {WOS:000088593300042},
      url          = {https://juser.fz-juelich.de/record/26938},
}