Muconate lactonizing enzymes (EC5.5.1.1, muconate cycloisomerase I, cis,cis-muconate-lactonizing enzyme, cis,cis-muconate cycloisomerase, muconate lactonizing enzyme, 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 dehalogenatingchloroaromatic 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]
References
^Ornston, L.N. (1966). "The conversion of catechol and protocatechuate to β-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway". J. Biol. Chem. 241: 3795–3799. PMID5330966.
^Ornston, L.N. (1970). "Conversion of catechol and protocatechuate to β-ketoadipate (Pseudomonas putida)". Methods Enzymol. 17A: 529–549.
^Sistrom, W.R. and Stanier, R.Y. (1954). "The mechanism of formation of β-ketoadipic acid by bacteria". J. Biol. Chem. 210: 821–836. PMID13211620.{{cite journal}}: CS1 maint: multiple names: authors list (link)
