MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: apo-citrate lyase phosphoribosyl-dephospho-CoA transferaseInferred from experiment: citX

In Pathway: citrate lyase activation

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: citrate lyase holo-[acyl-carrier protein] synthase

Enzyme Commission Synonyms: 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase, 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase, CitX, holo-ACP synthase (ambiguous), 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase, 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA transferase, 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase adenylyltransferase, holo-citrate lyase synthase (incorrect)

Standard Gibbs Free Energy (ΔrG in kcal/mol): -528.0613Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The γ-subunit of EC, citrate (pro-3S)-lyase, serves as an acyl-carrier protein (ACP) and contains the prosthetic group 2'-(5''-triphospho-α-D-ribosyl)-3'-dephospho-CoA [Schneider00a, Schneider02]. Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC, triphosphoribosyl-dephospho-CoA synthase [Schneider00a]. In the enzyme from E. coli, the prosthetic group is attached to serine-14 of the ACP via a phosphodiester bond.

Citations: [Schneider00]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Schneider00: Schneider K, Dimroth P, Bott M (2000). "Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group." FEBS Lett 2000;483(2-3);165-8. PMID: 11042274

Schneider00a: Schneider K, Dimroth P, Bott M (2000). "Biosynthesis of the prosthetic group of citrate lyase." Biochemistry 2000;39(31);9438-50. PMID: 10924139

Schneider02: Schneider K, Kastner CN, Meyer M, Wessel M, Dimroth P, Bott M (2002). "Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group." J Bacteriol 2002;184(9);2439-46. PMID: 11948157

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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