Muconate lactonizing enzyme
| Muconate cycloisomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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Muconate cycloisomerase oktamer, Thermotoga maritima | |||||||||
| Identifiers | |||||||||
| EC number | 5.5.1.1 | ||||||||
| CAS number | 9023-72-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Muconate lactonizing enzymes (EC 5.5.1.1, 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]
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. PMID 5330966.
- ↑ 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.
- ↑ Sistrom, W.R.; Stanier, R.Y. (1954). "The mechanism of formation of β-ketoadipic acid by bacteria". J. Biol. Chem. 210: 821–836. PMID 13211620.
External links
- cis,cis-muconate lactonizing enzyme at the US National Library of Medicine Medical Subject Headings (MeSH)
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