ArticleApplied and environmental microbiology2006
Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth.
Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- A novel positive selection system for plant transformation based on microbial biuret hydrolase and biuret.PloS one · 2026Article
- Triazine Herbicides Risk Management Strategies on Environmental and Human Health Aspects Using In-Silico Methods.International journal of molecular sciences · 2023Article
- Cyanuric Acid Biodegradation via Biuret: Physiology, Taxonomy, and Geospatial Distribution.Applied and environmental microbiology · 2020Article
- Structure and function of urea amidolyase.Bioscience reports · 2018Article
- Article
- The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent.Protein science : a publication of the Protein Society · 2016Article
- Ancient Evolution and Recent Evolution Converge for the Biodegradation of Cyanuric Acid and Related Triazines.Applied and environmental microbiology · 2016Review
- X-ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex.Applied and environmental microbiology · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of the amidase domain of allophanate hydrolase from Pseudomonas sp. strain ADP.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Atrazine biodegradation efficiency, metabolite detection, and trzD gene expression by enrichment bacterial cultures from agricultural soil.Journal of Zhejiang University. Science. B · 2013Article
- Structure and function of allophanate hydrolase.The Journal of biological chemistry · 2013Article
- The structure of allophanate hydrolase from Granulibacter bethesdensis provides insights into substrate specificity in the amidase signature family.Biochemistry · 2013Article
- A novel hydrolase identified by genomic-proteomic analysis of phenylurea herbicide mineralization by Variovorax sp. strain SRS16.Applied and environmental microbiology · 2011Article
- Evolution of catabolic pathways: Genomic insights into microbial s-triazine metabolism.Journal of bacteriology · 2007Review
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TrzF, the allophanate hydrolase from Enterobacter cloacae strain 99, was cloned, overexpressed in the presence of a chaperone protein, and purified to homogeneity. Native TrzF had a subunit molecular weight of 65,401 and a subunit stoichiometry of alpha(2) and did not contain significant levels of metals. TrzF showed time-dependent inhibition by phenyl phosphorodiamidate and is a member of the amidase signature protein family. TrzF was highly active in the hydrolysis of allophanate but was not active with urea, despite having been previously considered a urea amidolyase. TrzF showed lower activity with malonamate, malonamide, and biuret. The allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, was also shown to hydrolyze biuret slowly. Since biuret and allophanate are consecutive metabolites in cyanuric acid metabolism, the low level of biuret hydrolase activity can have physiological significance. A recombinant Escherichia coli strain containing atzD, encoding cyanuric acid hydrolase that produces biuret, and atzF grew slowly on cyanuric acid as a source of nitrogen. The amount of growth produced was consistent with the liberation of 3 mol of ammonia from cyanuric acid. In vitro, TrzF was shown to hydrolyze biuret to liberate 3 mol of ammonia. The biuret hydrolyzing activity of TrzF might also be physiologically relevant in native strains. E. cloacae strain 99 grows on cyanuric acid with a significant accumulation of biuret.
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