Muconate lactonizing enzyme

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Muconate cycloisomerase
Muconate cycloisomerase oktamer, Thermotoga maritima
EC number5.5.1.1
CAS number9023-72-7
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Muconate lactonizing enzymes (EC, muconate cycloisomerase I, cis,cis-muconate-lactonizing enzyme, cis,cis-muconate cycloisomerase, 4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing), CatB, MCI, MLE, 2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing)) are involved in the breakdown of lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates as a part of the β-ketoadipate pathway in soil microbes. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes. The bacterial MLEs belong to the enolase superfamily, several structures from which are known.[1][2][3]


  1. ^ Ornston LN (August 1966). "The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway". The Journal of Biological Chemistry. 241 (16): 3795–9. PMID 5330966.
  2. ^ Ornston, L.N. (1970). "Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549. doi:10.1016/0076-6879(71)17237-0.
  3. ^ Sistrom WR, Stanier RY (October 1954). "The mechanism of formation of beta-ketoadipic acid by bacteria". The Journal of Biological Chemistry. 210 (2): 821–36. PMID 13211620.

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