Ring-cleaving cyanuric acid amidohydrolase activity in the atrazine-mineralizingRalstonia basilensisM91-3

Autor:	David M. Stamper, Joseph A. Krzycki, Duongrutiai Nicomrat, Samuel J. Traina, Olli H. Tuovinen
Rok vydání:	2005
Předmět:	Cyanuric acid amidohydrolase activity biology Amidohydrolase Chemistry Pentamer Cyanuric acid amidohydrolase biology.organism_classification Biochemistry Catalysis Biuret test Hydrolysis chemistry.chemical_compound Ralstonia Organic chemistry Cyanuric acid Biotechnology
Zdroj:	Biocatalysis and Biotransformation. 23:387-396
ISSN:	1029-2446 1024-2422
DOI:	10.1080/10242420500372260
Popis:	The purpose of this study was to characterize the cyanuric acid amidohydrolase reaction in Ralstonia basilensis M91-3, an atrazine-mineralizing soil bacterium. This ring fission reaction is the last aromatic step in the degradative pathway of atrazine and other s-triazines. The products and molar stoichiometry of the cyanuric acid amidohydrolase reaction were one mol biuret (H2N·CO·NH·CO·NH2) and one mol CO2 per mol cyanuric acid hydrolyzed, as confirmed by 13C-NMR and gas chromatography. The optimum pH and temperature, substrate specificity, and kinetic parameters were also characterized for the purified enzyme. The native enzyme had two forms of different sizes, 204 kDa and 160 kDa. Each was a tetramer or pentamer of 44 kDa and 33 kDa, respectively.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ea1ce0518fc5808a6e5acb6760b43442 https://doi.org/10.1080/10242420500372260 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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