Abstract
2-Chloro-cis,cis-muconate, the product of ortho-cleavage of 3-chlorocatechol, was converted by purified preparations of the pJP4- and pAC27-encoded chloromuconate cycloisomerases (EC 5.5.1.7) to trans-dienelactone (trans-4-carboxymethylenebut-2-en-4-olide). The same compound was also formed when (+)-2-chloro- and (+)-5-chloromuconolactone were substrates of these enzyme preparations. Thus, the pJP4- and pAC27-encoded chloromuconate cycloisomerases are able to catalyze chloride elimination from (+)-5-chloromuconolactone. The ability to convert (+)-2-chloromuconolactone differentiates these enzymes from other groups of cycloisomerases.
MeSH Terms
4-Butyrolactone/analogs & derivatives,metabolism
Acinetobacter/enzymology
Adipates/metabolism
Alcaligenes/enzymology
Chromatography, High Pressure Liquid
Gram-Negative Aerobic Bacteria/enzymology
Intramolecular Lyases
Isomerases/metabolism
Sorbic Acid/analogs & derivatives,metabolism
Spectrophotometry
Chemicals
Adipates
5-chloromuconolactone
2-chloromuconic acid
2-chloromuconolactone
Isomerases
Intramolecular Lyases
chloromuconate cycloisomerase
4-Butyrolactone
Sorbic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Vollmer M D
Institut für Mikrobiologie, Universität Stuttgart, Germany.
Schlömann M
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