Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
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Escherichia coli K-12 substr. MG1655 Reaction: 2.7.7.61

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.7.7.61

Enzymes and Genes:
apo-citrate lyase phosphoribosyl-dephospho-CoA transferase Inferred from experiment : citX

In Pathway: citrate lyase activation

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: The right side is missing: H: 1

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)

Enzyme Commission Summary:
The γ-subunit of EC 4.1.3.6, 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, Schneider02a]. Synthesis and attachment of the prosthetic group requires the concerted action of this enzyme and EC 2.4.2.52, 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: [Schneider00b]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.7.7.61 , ENZYME:EC:2.7.7.61 , IUBMB-ExplorEnz:EC:2.7.7.61


References

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

Schneider00b: 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

Schneider02a: 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 184(9);2439-46. PMID: 11948157


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, biocyc14.