ArticleMolecular microbiology2013
Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Over the rainbow: structural characterization of the chromoproteins gfasPurple, amilCP, spisPink and eforRed.Acta crystallographica. Section D, Structural biology · 2022Article
- A procedure for removal of cyanuric acid in swimming pools using a cell-free thermostable cyanuric acid hydrolase.Journal of industrial microbiology & biotechnology · 2022Article
- Improved production of the non-native cofactor FScientific reports · 2021Article
- Cyanuric Acid Biodegradation via Biuret: Physiology, Taxonomy, and Geospatial Distribution.Applied and environmental microbiology · 2020Article
- The evolving story of AtzT, a periplasmic binding protein.Acta crystallographica. Section D, Structural biology · 2019Article
- Article
- An unexpected vestigial protein complex reveals the evolutionary origins of anThe Journal of biological chemistry · 2018Article
- Article
- 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
- Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel.Scientific reports · 2017Article
- Article
- Ancient Evolution and Recent Evolution Converge for the Biodegradation of Cyanuric Acid and Related Triazines.Applied and environmental microbiology · 2016Review
- Article
- Bacterial Cyanuric Acid Hydrolase for Water Treatment.Applied and environmental microbiology · 2015Article
- Identification of novel transaminases from a 12-aminododecanoic acid-metabolizing Pseudomonas strain.Microbial biotechnology · 2015Article
- 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
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyanuric acid hydrolase, AtzD, is the founding member of a newly identified family of ring-opening amidases. We report the first X-ray structure for this family, which is a novel fold (termed the 'Toblerone' fold) that likely evolved via the concatenation of monomers of the trimeric YjgF superfamily and the acquisition of a metal binding site. Structures of AtzD with bound substrate (cyanuric acid) and inhibitors (phosphate, barbituric acid and melamine), along with mutagenesis studies, allowed the identification of the active site. The AtzD monomer, active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. A single catalytic dyad (Ser85-Lys42) is hypothesized, based on biochemical evidence and crystallographic data. A plausible catalytic mechanism based on these observations is also presented. A comparison with a homology model of the related barbiturase, Bar, was used to infer the active-site residues responsible for substrate specificity, and the phylogeny of the 68 AtzD-like enzymes in the database were analysed in light of this structure-function relationship.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.