{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["180(24)"],"submitter":["Cha CJ"],"pubmed_abstract":["Rhodococcus rhodochrous N75 is able to metabolize 4-methylcatechol via a modified beta-ketoadipate pathway. This organism has been shown to activate 3-methylmuconolactone by the addition of coenzyme A (CoA) prior to hydrolysis of the butenolide ring. A lactone-CoA synthetase is induced by growth of R. rhodochrous N75 on p-toluate as a sole source of carbon. The enzyme has been purified 221-fold by ammonium sulfate fractionation, hydrophobic chromatography, gel filtration, and anion-exchange chromatography. The enzyme, termed 3-methylmuconolactone-CoA synthetase, has a pH optimum of 8.0, a native Mr of 128,000, and a subunit Mr of 62,000, suggesting that the enzyme is homodimeric. The enzyme is very specific for its 3-methylmuconolactone substrate and displays little or no activity with oth"],"journal":["Journal of bacteriology"],"pagination":["6668-73"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC107772"],"repository":["biostudies-literature"],"pubmed_title":["The modified beta-ketoadipate pathway in Rhodococcus rhodochrous N75: enzymology of 3-methylmuconolactone metabolism."],"pmcid":["PMC107772"],"pubmed_authors":["Cha CJ","Bruce NC","Cain RB"],"additional_accession":[]},"is_claimable":false,"name":"The modified beta-ketoadipate pathway in Rhodococcus rhodochrous N75: enzymology of 3-methylmuconolactone metabolism.","description":"Rhodococcus rhodochrous N75 is able to metabolize 4-methylcatechol via a modified beta-ketoadipate pathway. This organism has been shown to activate 3-methylmuconolactone by the addition of coenzyme A (CoA) prior to hydrolysis of the butenolide ring. A lactone-CoA synthetase is induced by growth of R. rhodochrous N75 on p-toluate as a sole source of carbon. The enzyme has been purified 221-fold by ammonium sulfate fractionation, hydrophobic chromatography, gel filtration, and anion-exchange chromatography. The enzyme, termed 3-methylmuconolactone-CoA synthetase, has a pH optimum of 8.0, a native Mr of 128,000, and a subunit Mr of 62,000, suggesting that the enzyme is homodimeric. The enzyme is very specific for its 3-methylmuconolactone substrate and displays little or no activity with oth","dates":{"release":"1998-01-01T00:00:00Z","publication":"1998 Dec","modification":"2025-04-04T09:50:12.327Z","creation":"2025-02-19T04:02:24.414Z"},"accession":"S-EPMC107772","cross_references":{"pubmed":["9852013"],"doi":["10.1128/JB.180.24.6668-6673.1998"]}}