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

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dc.contributor.authorGriffin, M.D.W.
dc.contributor.authorBillakanti, J.M.
dc.contributor.authorWason, A.
dc.contributor.authorKeller, S.
dc.contributor.authorMertens, H.D.T.
dc.contributor.authorAtkinson, S.C.
dc.contributor.authorDobson, R.C.J.
dc.contributor.authorPerugini, M.A.
dc.contributor.authorGerrard, J.A.
dc.contributor.authorPearce, F.G.
dc.date.accessioned2013-07-29T22:15:22Z
dc.date.available2013-07-29T22:15:22Z
dc.date.issued2012en
dc.description.abstractIn 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)-lysine bound at a cleft between two monomers, highlighting the allosteric site; however, unlike previous studies, binding is not accompanied by conformational changes, suggesting that binding may cause changes in protein dynamics rather than large conformation changes. DHDPR from A. thaliana (At-DHDPR2) has similar specificity for both NADH and NADPH during catalysis, and has tighter binding of substrate than has previously been reported. While all known bacterial DHDPR enzymes have a tetrameric structure, analytical ultracentrifugation, and scattering data unequivocally show that At-DHDPR2 exists as a dimer in solution. The exact arrangement of the dimeric protein is as yet unknown, but ab initio modelling of x-ray scattering data is consistent with an elongated structure in solution, which does not correspond to any of the possible dimeric pairings observed in the X-ray crystal structure of DHDPR from other organisms. This increased knowledge of the structure and function of plant lysine biosynthetic enzymes will aid future work aimed at improving primary production.en
dc.identifier.citationGriffin, M.D.W., Billakanti, J.M., Wason, A., Keller, S., Mertens, H.D.T., Atkinson, S.C., Dobson, R.C.J., Perugini, M.A., Gerrard, J.A., Pearce, F.G. (2012) Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana. PLoS One, 7(7), pp. e40318.en
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0040318
dc.identifier.urihttp://hdl.handle.net/10092/8009
dc.language.isoen
dc.publisherUniversity of Canterbury. Biological Sciencesen
dc.publisherUniversity of Canterbury. Biomolecular Interaction Centreen
dc.rights.urihttps://hdl.handle.net/10092/17651en
dc.subject.anzsrcFields of Research::30 - Agricultural, veterinary and food sciences::3004 - Crop and pasture production::300404 - Crop and pasture biochemistry and physiologyen
dc.subject.anzsrcFields of Research::31 - Biological sciences::3101 - Biochemistry and cell biology::310106 - Enzymesen
dc.subject.anzsrcFields of Research::31 - Biological sciences::3101 - Biochemistry and cell biology::310113 - Synthetic biologyen
dc.subject.anzsrcField of Research::06 - Biological Sciences::0607 - Plant Biology::060705 - Plant Physiologyen
dc.titleCharacterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thalianaen
dc.typeJournal Article
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