ExplorEnz: EC 5.5.1.1

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5.5.1.1

Accepted name:

muconate cycloisomerase

Reaction:

(+)-muconolactone = cis,cis-muconate

For diagram of benzoate metabolism, click here

Glossary:

(+)-muconolactone = (S)-(2,5-dihydro-5-oxofuran-2-yl)-acetate
cis,cis-muconate = cis,cis-hexadienedioate = (2Z,4Z)-hexa-2,4-dienedioate

Other name(s):

muconate cycloisomerase I; cis,cis-muconate-lactonizing enzyme; cis,cis-muconate cycloisomerase; muconate lactonizing enzyme; 4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing); CatB; MCI; 2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing); 2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)

Systematic name:

(+)-muconolactone lyase (ring-opening)

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:

BRENDA, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-72-7

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

[EC 5.5.1.1 created 1961]