Structural highlights
Function
ATZA_PSESD Hydrolytically dechlorinates atrazine to hydroxyatrazine. Dechlorinates also simazine, and desethylatrazine but is not active with melamine, terbutylazine, or desethyldesisopropylatrazine.[1]
Publication Abstract from PubMed
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.
The structure of the hexameric atrazine chlorohydrolase AtzA.,Peat TS, Newman J, Balotra S, Lucent D, Warden AC, Scott C Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):710-20. doi:, 10.1107/S1399004715000619. Epub 2015 Feb 26. PMID:25760618[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Souza ML, Sadowsky MJ, Wackett LP. Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization. J Bacteriol. 1996 Aug;178(16):4894-900. PMID:8759853
- ↑ Peat TS, Newman J, Balotra S, Lucent D, Warden AC, Scott C. The structure of the hexameric atrazine chlorohydrolase AtzA. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):710-20. doi:, 10.1107/S1399004715000619. Epub 2015 Feb 26. PMID:25760618 doi:http://dx.doi.org/10.1107/S1399004715000619
