Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073

Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric a...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 2009-11, Vol.75 (22), p.6986-6991
Main Authors: Li, Qingyan, Seffernick, Jennifer L, Sadowsky, Michael J, Wackett, Lawrence P
Format: Article
Language:English
Subjects:
Bacteria - classification
Bacteria - enzymology
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biochemistry
Biological and medical sciences
Chelating Agents - chemistry
Chemical compounds
Cloning, Molecular
Cofactors
E coli
Enzyme Stability
Enzymes
Enzymology and Protein Engineering
Escherichia coli
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydrolases - chemistry
Hydrolases - genetics
Hydrolases - isolation & purification
Hydrolases - metabolism
Metabolism
Metals - analysis
Metals - chemistry
Microbiology
Microorganisms
Phylogeny
Substrate Specificity
Temperature
Triazines - metabolism
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Summary:Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.
ISSN:0099-2240
1098-5336
1098-6596
DOI:10.1128/AEM.01605-09