Evidence map›Paper›PMID 22792278›Full record

ArticlePloS one2012

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

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

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
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  15. Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
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  20. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Michael D W GriffinDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria, Australia.
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
University of Canterbury · NZUniversity of Melbourne · AUAustralian Synchrotron · AULa Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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)-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.

Indexed as

Allosteric SiteArabidopsisArabidopsis ProteinsBiosynthetic PathwaysCrystallography, X-RayDihydrodipicolinate ReductaseHydro-LyasesKineticsLightLysineModels, MolecularProtein Interaction Domains and MotifsProtein Structure, QuaternaryScattering, Small AngleStructural Homology, Protein4-hydroxy-tetrahydrodipicolinate synthaseArabidopsis ProteinsDihydrodipicolinate ReductaseHydro-LyasesLysine

Identifiers

PMID22792278
PMCPMC3390394
OpenAlexW2071644882

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.