Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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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
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Escherichia coli K-12 substr. MG1655 Reaction: 4.1.3.6

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Composite Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.1.3.6

Enzymes and Genes:
citrate lyase Inferred from experiment : citD , citF , citE

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: Balanced.

Enzyme Commission Primary Name: citrate (pro-3S)-lyase

Enzyme Commission Synonyms: citrase, citratase, citritase, citridesmolase, citrate aldolase, citric aldolase, citrate lyase, citrate oxaloacetate-lyase, citrate oxaloacetate-lyase [(pro-3S)-CH2COO-->acetate]

Sub-reactions:
an acetyl-[holo citrate lyase acyl-carrier protein] + citrate → a citryl-[holo citrate lyase acyl-carrier protein] + acetate ,
a citryl-[holo citrate lyase acyl-carrier protein] → oxaloacetate + an acetyl-[holo citrate lyase acyl-carrier protein]

Summary:
This overall reaction is carried out by the citrate lyase multienzyme complex. The reaction proceeds in two steps, each one catalyzed by a separate subunit of the enzyme complex.

Enzyme Commission Summary:
The enzyme can be dissociated into components, two of which are identical with EC 2.8.3.10, citrate CoA-transferase and EC 4.1.3.34, citryl-CoA lyase. EC 3.1.2.16, citrate lyase deacetylase deacetylates and inactivates the enzyme.

Citations: [Dimroth77, DAGLEY55]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:4.1.3.6 , ENZYME:EC:4.1.3.6 , IUBMB-ExplorEnz:EC:4.1.3.6


References

DAGLEY55: DAGLEY S, DAWES EA (1955). "Citridesmolase: its properties and mode of action." Biochim Biophys Acta 17(2);177-84. PMID: 13239657

Dimroth77: Dimroth P, Loyal R, Eggerer H (1977). "Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate." Eur J Biochem 80(2);479-88. PMID: 336371


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 Sat Dec 20, 2014, biocyc14.