MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Cupriavidus sp. PS12 : chloromuconate cycloisomerase Inferred from experiment
Pseudomonas putida : muconate cycloisomerase Inferred from experiment : catB
Pseudomonas reinekei : muconate cycloisomerase I Inferred from experiment : salC
muconate cycloisomerase Inferred from experiment : catB

In Pathway: catechol degradation to β-ketoadipate

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

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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): -1.4282227 Inferred 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 SRI International Pathway Tools version 19.0 on Tue Oct 13, 2015, BIOCYC11A.