Journal article

Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana

MDW Griffin, JM Billakanti, A Wason, S Keller, HDT Mertens, SC Atkinson, RCJ Dobson, MA Perugini, JA Gerrard, FG Pearce

Plos One | PUBLIC LIBRARY SCIENCE | Published : 2012

Abstract

In plants, the lysine biosynthetic pathway is an attractive target for both the development of herbicides and increasing the nutritional value of crops given that lysine is a limiting amino acid in cereals. Dihydrodipicolinate synthase (DHDPS) and dihydrodipicolinate reductase (DHDPR) catalyse the first two committed steps of lysine biosynthesis. Here, we carry out for the first time a comprehensive characterisation of the structure and activity of both DHDPS and DHDPR from Arabidopsis thaliana. The A. thaliana DHDPS enzyme (At-DHDPS2) has similar activity to the bacterial form of the enzyme, but is more strongly allosterically inhibited by (S)-lysine. Structural studies of At-DHDPS2 show (S..

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University of Melbourne Researchers

Grants

Awarded by Defense Threat Reduction Agency


Funding Acknowledgements

This work was supported in part by the Defense Threat Reduction Agency (W911NF-07-1-0073 and AB07CBT004) and in part by the Foundation of Research, Science and Technology. Travel to the Australian Synchrotron was funded by the New Zealand Synchrotron Group. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.