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Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store

MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Cupriavidus sp. PS12: chloromuconate cycloisomeraseInferred from experiment
Pseudomonas putida: muconate cycloisomeraseInferred from experiment: catB
Pseudomonas reinekei: muconate cycloisomerase IInferred from experiment: salC
muconate cycloisomeraseInferred from experiment: catB

In Pathway: catechol degradation to β-ketoadipate

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: muconate cycloisomerase

Enzyme Commission Synonyms: muconate cycloisomerase I, cis,cis-muconate-lactonizing enzyme, cis,cis-muconate cycloisomerase, muconate lactonizing enzyme, 4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing), CatB, MCI

Standard Gibbs Free Energy (ΔrG in kcal/mol): -1.4282227Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Requires Mn2+. Also acts (in the reverse reaction) on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-hexadienedioate. Not identical with EC (chloromuconate cycloisomerase) or EC (dichloromuconate cycloisomerase).

Citations: [Sistrom54, Ornston66]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R03959, Rhea:10640

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O33946, UniProt:RELATED-TO:O33949, UniProt:RELATED-TO:P08310, UniProt:RELATED-TO:Q9Z9Y1


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

Ornston66: Ornston LN (1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway." J Biol Chem 241(16);3795-9. PMID: 5330966

Sistrom54: Sistrom WR, Stanier RY (1954). "The mechanism of formation of beta-ketoadipic acid by bacteria." J Biol Chem 210(2);821-36. PMID: 13211620

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
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.