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001     26938
005     20200423203420.0
024 7 _ |a pmid:10924139
|2 pmid
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024 7 _ |a 2128/722
|2 Handle
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|2 altmetric
037 _ _ |a PreJuSER-26938
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Schneider, K.
|0 P:(DE-HGF)0
|b 0
245 _ _ |a Biosynthesis of the prosthetic group of citrate lyase
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2000
300 _ _ |a 9438 - 9450
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemistry
|x 0006-2960
|0 798
|v 39
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Entwicklung von Mikroorganismen für die Herstellung von Primärmetaboliten
|c 41.30.0
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK91
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Acyl Carrier Protein: biosynthesis
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Apoproteins: biosynthesis
650 _ 2 |2 MeSH
|a Carbon-Sulfur Ligases: biosynthesis
650 _ 2 |2 MeSH
|a Carbon-Sulfur Ligases: genetics
650 _ 2 |2 MeSH
|a Coenzyme A: biosynthesis
650 _ 2 |2 MeSH
|a Enzyme Precursors: metabolism
650 _ 2 |2 MeSH
|a Escherichia coli: enzymology
650 _ 2 |2 MeSH
|a Escherichia coli: genetics
650 _ 2 |2 MeSH
|a Genes, Bacterial
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Multienzyme Complexes: biosynthesis
650 _ 2 |2 MeSH
|a Multienzyme Complexes: chemistry
650 _ 2 |2 MeSH
|a Multienzyme Complexes: genetics
650 _ 2 |2 MeSH
|a Multigene Family
650 _ 2 |2 MeSH
|a Operon
650 _ 2 |2 MeSH
|a Oxo-Acid-Lyases: biosynthesis
650 _ 2 |2 MeSH
|a Oxo-Acid-Lyases: chemistry
650 _ 2 |2 MeSH
|a Oxo-Acid-Lyases: genetics
650 _ 2 |2 MeSH
|a Structure-Activity Relationship
650 _ 7 |0 0
|2 NLM Chemicals
|a Acyl Carrier Protein
650 _ 7 |0 0
|2 NLM Chemicals
|a Apoproteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Enzyme Precursors
650 _ 7 |0 0
|2 NLM Chemicals
|a Multienzyme Complexes
650 _ 7 |0 3633-59-8
|2 NLM Chemicals
|a dephosphocoenzyme A
650 _ 7 |0 85-61-0
|2 NLM Chemicals
|a Coenzyme A
650 _ 7 |0 EC 4.1.3.-
|2 NLM Chemicals
|a Oxo-Acid-Lyases
650 _ 7 |0 EC 4.1.3.6
|2 NLM Chemicals
|a citrate (pro-3S)-lyase
650 _ 7 |0 EC 6.2.-
|2 NLM Chemicals
|a Carbon-Sulfur Ligases
650 _ 7 |0 EC 6.2.1.20
|2 NLM Chemicals
|a long-chain-fatty-acid-(acyl-carrier-protein) ligase
650 _ 7 |0 EC 6.2.1.22
|2 NLM Chemicals
|a citrate (pro-3S)-lyase ligase
650 _ 7 |a J
|2 WoSType
700 1 _ |a Dimroth, B. M.
|0 P:(DE-HGF)0
|b 1
700 1 _ |a Bott, M.
|0 P:(DE-Juel1)128943
|b 2
|u FZJ
773 _ _ |g Vol. 39, p. 9438 - 9450
|p 9438 - 9450
|q 39<9438 - 9450
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 39
|y 2000
|x 0006-2960
856 4 _ |u https://juser.fz-juelich.de/record/26938/files/19821.pdf
|y OpenAccess
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913 1 _ |k 41.30.0
|v Entwicklung von Mikroorganismen für die Herstellung von Primärmetaboliten
|l Biotechnologie
|b Lebenswissenschaften
|0 G:(DE-Juel1)FUEK91
|x 0
914 1 _ |y 2000
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
915 _ _ |2 StatID
|0 StatID:(DE-HGF)0510
|a OpenAccess
920 1 _ |k IBT
|l Institut für Biotechnologie
|d 31.12.2000
|g IBT
|0 I:(DE-Juel1)VDB184
|x 0
970 _ _ |a VDB:(DE-Juel1)19821
980 _ _ |a VDB
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980 _ _ |a journal
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980 _ _ |a UNRESTRICTED
980 _ _ |a FullTexts
980 1 _ |a FullTexts

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