X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC

@article{Balotra2015XRaySA,
  title={X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC},
  author={Sahil Balotra and Andrew C. Warden and Janet Newman and Lyndall J. Briggs and Colin Scott and Thomas S. Peat},
  journal={PLoS ONE},
  year={2015},
  volume={10}
}
The N-isopropylammelide isopropylaminohydrolase from Pseudomonas sp. strain ADP, AtzC, provides the third hydrolytic step in the mineralization of s-triazine herbicides, such as atrazine. We obtained the X-ray crystal structure of AtzC at 1.84 Å with a weak inhibitor bound in the active site and then used a combination of in silico docking and site-directed mutagenesis to understand the interactions between AtzC and its substrate, isopropylammelide. The substitution of an active site histidine… 
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Purification, characterization, and catalytic mechanism of N-Isopropylammelide isopropylaminohydrolase (AtzC) involved in the degradation of s-triazine herbicides.
An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme
TLDR
It is proposed that AtzEG was likely recruited into the cyanuric acid–mineralizing pathway from an ancestral glutamine transamidosome that required protein–protein interactions to enforce the exclusion of solvent from the transamidation reaction.
The evolving story of AtzT, a periplasmic binding protein
TLDR
The structure of AtzT, which is thought to be involved in atrazine uptake in bacteria, was solved by SAD phasing using an ethylmercury phosphate derivative to replace guanine with 2-hydroxyatrazine.
Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841
TLDR
The structure of the inactive Cys175Ser BiuH variant with substrate bound in the active site revealed that an active site cysteine (Cys175), aspartic acid (Asp36) and lysine (Lys142) form a catalytic triad, which is consistent with biochemical studies ofBiuH variants.
Bacterial catabolism of s-triazine herbicides: biochemistry, evolution and application.

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