ArticleActa crystallographica. Section D, Biological crystallography2015
The structure of the hexameric atrazine chlorohydrolase AtzA.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Kinetic isotope effects of C and N indicate different transformation mechanisms between atzA- and trzN-harboring strains in dechlorination of atrazine.Biodegradation · 2022Article
- Structural basis for the hydrolytic dehalogenation of the fungicide chlorothalonil.The Journal of biological chemistry · 2020Article
- Biochemical and Genetic Analysis of 4-Hydroxypyridine Catabolism inMicroorganisms · 2020Article
- Evolution of new enzymes by gene duplication and divergence.The FEBS journal · 2020Review
- The evolving story of AtzT, a periplasmic binding protein.Acta crystallographica. Section D, Structural biology · 2019Article
- In silico design of potentially functional artificial metallo-haloalkane dehalogenase containing catalytic zinc.3 Biotech · 2018Article
- An unexpected vestigial protein complex reveals the evolutionary origins of anThe Journal of biological chemistry · 2018Article
- Dehalogenases: From Improved Performance to Potential Microbial Dehalogenation Applications.Molecules (Basel, Switzerland) · 2018Review
- Article
- X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.PloS one · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Atrazine chlorohydrolase (AtzA) was discovered and purified in the early 1990s from soil that had been exposed to the widely used herbicide atrazine. It was subsequently found that this enzyme catalyzes the first and necessary step in the breakdown of atrazine by the soil organism Pseudomonas sp. strain ADP. Although it has taken 20 years, a crystal structure of the full hexameric form of AtzA has now been obtained. AtzA is less well adapted to its physiological role (i.e. atrazine dechlorination) than the alternative metal-dependent atrazine chlorohydrolase (TrzN), with a substrate-binding pocket that is under considerable strain and for which the substrate is a poor fit.
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Registered trials
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