X-Ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC

Sahil Balotra, Andrew C. Warden, Janet Newman, Lyndall J. Briggs, Colin Scott, Thomas S. Peat

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5 Citations (Scopus)
3 Downloads (Pure)

Abstract

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 residue (His249) for an alanine abolished the enzyme's catalytic activity. We propose a plausible catalytic mechanism, consistent with the biochemical and crystallographic data obtained that is similar to that found in carbonic anhydrase and other members of subtype III of the amidohydrolase family.

Original languageEnglish
Article numbere0137700
Pages (from-to)1-15
Number of pages15
JournalPLoS ONE
Volume10
Issue number9
DOIs
Publication statusPublished - 21 Sep 2015
Externally publishedYes

Bibliographical note

Copyright the Author(s) 2015. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

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