Advanced search
Publication Cover
Biocatalysis and Biotransformation Volume 23, 2005 - Issue 6
Submit an article Journal homepage
40
Views
8
CrossRef citations to date
0
Altmetric
ORIGINAL ARTICLE

Ring-cleaving cyanuric acid amidohydrolase activity in the atrazine-mineralizing Ralstonia basilensis M91-3

David M. Stamper Biological Sciences Group, NAVSEA Warfare Centers, Carderock Division, West Bethesda, MD, 20817, USA
,
Joseph A. Krzycki Department of Microbiology, Ohio State University, 484 W. 12th Avenue, Columbus, OH, 43210, USA
,
Duongrutiai Nicomrat Department of Microbiology, Ohio State University, 484 W. 12th Avenue, Columbus, OH, 43210, USA
,
David M. Stamper Biological Sciences Group, NAVSEA Warfare Centers, Carderock Division, West Bethesda, MD, 20817, USA
,
Joseph A. Krzycki Department of Microbiology, Ohio State University, 484 W. 12th Avenue, Columbus, OH, 43210, USA
,
Duongrutiai Nicomrat Department of Microbiology, Ohio State University, 484 W. 12th Avenue, Columbus, OH, 43210, USA
,
Samuel J. Traina Sierra Nevada Research Institute, University of California-Merced, P.O. Box 2039, Merced, CA, 95433, USA
&
Olli H. Tuovinen Department of Microbiology, Ohio State University, 484 W. 12th Avenue, Columbus, OH, 43210, USACorrespondence[email protected]
 show all
Pages 387-396 | Received 13 Jun 2005, Published online: 11 Jul 2009
 
Sample our Bioscience journals, sign in here to start your access, Latest two full volumes FREE to you for 14 days

Abstract

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.

Log in via your institution

Access through your institution

Log in to Taylor & Francis Online

Restore content access

Restore content access for purchases made as guest
Purchase options * Save for later

PDF download + Online access

  • 48 hours access to article PDF & online version
  • Article PDF can be downloaded
  • Article PDF can be printed
USD 61.00 Add to cart

Issue Purchase

  • 30 days online access to complete issue
  • Article PDFs can be downloaded
  • Article PDFs can be printed
USD 791.00 Add to cart

* Local tax will be added as applicable

Related Research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.