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

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 f...

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Autores principales:	Michael D W Griffin, Jagan M Billakanti, Akshita Wason, Sabrina Keller, Haydyn D T Mertens, Sarah C Atkinson, Renwick C J Dobson, Matthew A Perugini, Juliet A Gerrard, Frederick Grant Pearce
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1ea922ff58024eaf9855c830510354cf
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spelling	oai:doaj.org-article:1ea922ff58024eaf9855c830510354cf2021-11-18T07:13:21ZCharacterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.1932-620310.1371/journal.pone.0040318https://doaj.org/article/1ea922ff58024eaf9855c830510354cf2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22792278/?tool=EBIhttps://doaj.org/toc/1932-6203In 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.Michael D W GriffinJagan M BillakantiAkshita WasonSabrina KellerHaydyn D T MertensSarah C AtkinsonRenwick C J DobsonMatthew A PeruginiJuliet A GerrardFrederick Grant PearcePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e40318 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Michael D W Griffin Jagan M Billakanti Akshita Wason Sabrina Keller Haydyn D T Mertens Sarah C Atkinson Renwick C J Dobson Matthew A Perugini Juliet A Gerrard Frederick Grant Pearce Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
description	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)-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.
format	article
author	Michael D W Griffin Jagan M Billakanti Akshita Wason Sabrina Keller Haydyn D T Mertens Sarah C Atkinson Renwick C J Dobson Matthew A Perugini Juliet A Gerrard Frederick Grant Pearce
author_facet	Michael D W Griffin Jagan M Billakanti Akshita Wason Sabrina Keller Haydyn D T Mertens Sarah C Atkinson Renwick C J Dobson Matthew A Perugini Juliet A Gerrard Frederick Grant Pearce
author_sort	Michael D W Griffin
title	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
title_short	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
title_full	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
title_fullStr	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
title_full_unstemmed	Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.
title_sort	characterisation of the first enzymes committed to lysine biosynthesis in arabidopsis thaliana.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/1ea922ff58024eaf9855c830510354cf
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Characterisation of the first enzymes committed to lysine biosynthesis in Arabidopsis thaliana.

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