ArticleApplied and environmental microbiology2015
X-ray structure of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Investigation of the Persistence, Toxicological Effects, and Ecological Issues of S-Triazine Herbicides and Their Biodegradation Using Emerging Technologies: A Review.Microorganisms · 2023Review
- Identification of Tse8 as a Type VI secretion system toxin from Pseudomonas aeruginosa that targets the bacterial transamidosome to inhibit protein synthesis in prey cells.Nature microbiology · 2021Article
- The evolving story of AtzT, a periplasmic binding protein.Acta crystallographica. Section D, Structural biology · 2019Article
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- An unexpected vestigial protein complex reveals the evolutionary origins of anThe Journal of biological chemistry · 2018Article
- Structure and function of urea amidolyase.Bioscience reports · 2018Article
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- Article
- High-Resolution X-Ray Structures of Two Functionally Distinct Members of the Cyclic Amide Hydrolase Family of Toblerone Fold Enzymes.Applied and environmental microbiology · 2017Article
- 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
- The structure of the hexameric atrazine chlorohydrolase AtzA.Acta crystallographica. Section D, Biological crystallography · 2015Article
- X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.PloS one · 2015Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activity of the allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, provides the final hydrolytic step for the mineralization of s-triazines, such as atrazine and cyanuric acid. Indeed, the action of AtzF provides metabolic access to two of the three nitrogens in each triazine ring. The X-ray structure of the N-terminal amidase domain of AtzF reveals that it is highly homologous to allophanate hydrolases involved in a different catabolic process in other organisms (i.e., the mineralization of urea). The smaller C-terminal domain does not appear to have a physiologically relevant catalytic function, as reported for the allophanate hydrolase of Kluyveromyces lactis, when purified enzyme was tested in vitro. However, the C-terminal domain does have a function in coordinating the quaternary structure of AtzF. Interestingly, we also show that AtzF forms a large, ca. 660-kDa, multienzyme complex with AtzD and AtzE that is capable of mineralizing cyanuric acid. The function of this complex may be to channel substrates from one active site to the next, effectively protecting unstable metabolites, such as allophanate, from solvent-mediated decarboxylation to a dead-end metabolic product.
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