Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 5.5.1.1

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

EC Number: 5.5.1.1

Enzymes and Genes:
muconate cycloisomerase Inferred from experiment : catB ( Pseudomonas reinekei )
muconate cycloisomerase I Inferred from experiment : salC ( Pseudomonas reinekei )
chloromuconate cycloisomerase Inferred from experiment ( Cupriavidus sp. PS12 )
muconate cycloisomerase Inferred from experiment : catB ( Pseudomonas putida )

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-hexadienedioate and, very slowly, on cis,trans-hexadienedioate. Not identical with EC 5.5.1.7 (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).

Citations: [SISTROM54, Ornston66a]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R03959 , Rhea:10640

Relationship Links: BRENDA:EC:5.5.1.1 , ENZYME:EC:5.5.1.1 , IUBMB-ExplorEnz:EC:5.5.1.1 , UniProt:RELATED-TO:O33946 , UniProt:RELATED-TO:O33949 , UniProt:RELATED-TO:P08310 , UniProt:RELATED-TO:Q9Z9Y1


References

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

Ornston66a: 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 18.5 on Thu Nov 27, 2014, BIOCYC14B.