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Information on EC 2.4.2.52 - triphosphoribosyl-dephospho-CoA synthase and Organism(s) Escherichia coli and UniProt Accession P77231
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EC Tree
2.4.2.52 triphosphoribosyl-dephospho-CoA synthaseIUBMB Comments
ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new alpha (1''->2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (gamma-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase .
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase, ATP:dephospho-CoA 5-triphosphoribosyl transferase, CitG, EC 2.7.8.25, MdcB, synthetase, 2'-(5''-triphosphoribosyl)-3'-dephospho-coenzyme A, triphosphoribosyldephospho-CoA synthase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-(5''-triphosphoribosyl)-3-dephospho-CoA synthase
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ATP:dephospho-CoA 5-triphosphoribosyl transferase
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CitG
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synthetase, 2'-(5''-triphosphoribosyl)-3'-dephospho-coenzyme A
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triphosphoribosyldephospho-CoA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 3'-dephospho-CoA = 2'-(5-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA is the prosthetic group precursor of the gamma-subunit of the citrate lyase EC 4.1.3.6
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of 3-dephospho-CoA
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substituted phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:3'-dephospho-CoA 5-triphospho-alpha-D-ribosyltransferase
ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new alpha (1''->2') glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2'-(5-triphosphoribosyl)-3'-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (gamma-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4].
CAS REGISTRY NUMBER
COMMENTARY
313345-38-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3'-dephospho-CoA
2'-(5-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine
CitG catalyzes the conversion of ATP and dephospho-CoA to adenine and 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA, the predicted precursor of the prosthetic group of the gamma-subunit of citrate lyase EC 4.1.3.6. This precursor is transferred by CitX to apo-acyl carrier protein, yielding holo-acyl carrier protein
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ATP + 3'-dephospho-CoA
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + adenine
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ATP + 3'-dephospho-CoA
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + adenine
ATP cannot be replaced by CTP, GTP or UTP
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additional information
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holo-acyl carrier protein 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. The conversion of apo-cyl carrier protein into holo-cyl carrier protein is achieved in vitro by incubation of apo-cyl carrier protein with proteins CitX, CitG, ATP, and dephospho-CoA. ATP cannot be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-cyl carrier protein is formed. It is not possible to further convert AMP-cyl carrier protein to holo-cyl carrier protein by subsequent incubation with CitG and dephospho-CoA
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additional information
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holo-acyl carrier protein 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. The conversion of apo-cyl carrier protein into holo-cyl carrier protein is achieved in vitro by incubation of apo-cyl carrier protein with proteins CitX, CitG, ATP, and dephospho-CoA. ATP cannot be substituted with GTP, CTP, UTP, ADP, or AMP. In the absence of CitG or dephospho-CoA, AMP-cyl carrier protein is formed. It is not possible to further convert AMP-cyl carrier protein to holo-cyl carrier protein by subsequent incubation with CitG and dephospho-CoA
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3'-dephospho-CoA
2'-(5''-triphosphoribosyl)-3'-dephospho-CoA + adenine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, K.; Dimroth, P.; Bott, M.
Biosynthesis of the prosthetic group of citrate lyase
Biochemistry
39
9438-9450
2000
Escherichia coli, Escherichia coli (P77231), Klebsiella pneumoniae (P45414)
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