EC 5.5.1.1 - Muconate cycloisomerase

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IntEnz Enzyme Nomenclature
EC 5.5.1.1

Names

Accepted name:
muconate cycloisomerase
Other names:
4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing)
cis,cis-muconate cycloisomerase
cis,cis-muconate-lactonizing enzyme
muconate cycloisomerase I
muconate lactonizing enzyme
cis,cis-muconate lactonizing enzyme I
CatB
MCl
2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)
Systematic name:
2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)

Reaction

Cofactor

Comments:

Requires Mn2+. Also acts (in the reverse reaction) on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-muconate. Not identical with EC 5.5.1.7 (chloromuconate cycloisomerase) or EC 5.5.1.11 (dichloromuconate cycloisomerase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00706
Structural data: CSA , EC2PDB
Gene Ontology: GO:0018849
CAS Registry Number: 9023-72-7
UniProtKB/Swiss-Prot:

References

  1. Ornston, L.N.
    The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway.
    J. Biol. Chem. 241: 3795-3799 (1966). [PMID: 5330966]
  2. Ornston, L.N.
    Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida).
    Methods Enzymol. 17A: 529-549 (1970).
  3. Sistrom, W.R. and Stanier, R.Y.
    The mechanism of formation of β-ketoadipic acid by bacteria.
    J. Biol. Chem. 210: 821-836 (1954). [PMID: 13211620]

[EC 5.5.1.1 created 1961]