Details zur Publikation |
| Kategorie | Textpublikation |
| Referenztyp | Zeitschriften |
| DOI | 10.1111/1462-2920.13875 |
| Volltext | Akzeptiertes Manuskript |
| Titel (primär) | Phthaloyl-coenzyme A decarboxylase from Thauera chlorobenzoica: the prenylated flavin-, K+- and Fe2+-dependent key enzyme of anaerobic phthalate degradation |
| Autor | Mergelsberg, M.; Willistein, M.; Meyer, H.; Stärk, H.-J.; Bechtel, D.F.; Pierik, A.J.; Boll, M. |
| Quelle | Environmental Microbiology |
| Erscheinungsjahr | 2017 |
| Department | ANA |
| Band/Volume | 19 |
| Heft | 9 |
| Seite von | 3734 |
| Seite bis | 3744 |
| Sprache | englisch |
| Supplements | https://onlinelibrary.wiley.com/action/downloadSupplement?doi=10.1111%2F1462-2920.13875&attachmentId=183567801 |
| UFZ Querschnittsthemen | RU4; |
| Abstract | The degradation of the industrially produced and environmentally relevant phthalate esters by microorganisms is initiated by the hydrolysis to alcohols and phthalate (1,2-dicarboxybenzene). In the absence of oxygen the further degradation of phthalate proceeds via activation to phthaloyl-CoA followed by decarboxylation to benzoyl-CoA. Here, we report on the first purification and characterization of a phthaloyl-CoA decarboxylase (PCD) from the denitrifying Thauera chlorobenzoica. Hexameric PCD belongs to the UbiD-family of (de)carboxylases and contains prenylated FMN (prFMN), K+ and, unlike other UbiD-like enzymes, Fe2+ as cofactors. The latter is suggested to be involved in oxygen-independent electron-transfer during oxidative prFMN maturation. Either oxidation to the Fe3+-state in air or removal of K+ by desalting resulted in >92% loss of both, prFMN and decarboxylation activity suggesting the presence of an active site prFMN/Fe2+/K+-complex in PCD. The PCD-catalysed reaction was essentially irreversible: neither carboxylation of benzoyl-CoA in the presence of 2 M bicarbonate, nor an isotope exchange of phthaloyl-CoA with 13C-bicarbonate was observed. PCD differs in many aspects from prFMN-containing UbiD-like decarboxylases and serves as a biochemically accessible model for the large number of UbiD-like (de)carboxylases that play key roles in the anaerobic degradation of environmentally relevant aromatic pollutants. |
| dauerhafte UFZ-Verlinkung | https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=19285 |
| Mergelsberg, M., Willistein, M., Meyer, H., Stärk, H.-J., Bechtel, D.F., Pierik, A.J., Boll, M. (2017): Phthaloyl-coenzyme A decarboxylase from Thauera chlorobenzoica: the prenylated flavin-, K+- and Fe2+-dependent key enzyme of anaerobic phthalate degradation Environ. Microbiol. 19 (9), 3734 - 3744 10.1111/1462-2920.13875 |
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