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X Demographics
Mendeley readers
Attention Score in Context
| Title |
Characterisation of the First Enzymes Committed to Lysine Biosynthesis in Arabidopsis thaliana
|
|---|---|
| Published in |
PLOS ONE, July 2012
|
| DOI | 10.1371/journal.pone.0040318 |
| Pubmed ID | |
| Authors |
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 |
| 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. |
X Demographics
The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 1 | 100% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Members of the public | 1 | 100% |
Mendeley readers
The data shown below were compiled from readership statistics for 32 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Mexico | 1 | 3% |
| India | 1 | 3% |
| Brazil | 1 | 3% |
| Unknown | 29 | 91% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 9 | 28% |
| Student > Master | 6 | 19% |
| Student > Bachelor | 6 | 19% |
| Student > Postgraduate | 3 | 9% |
| Other | 1 | 3% |
| Other | 2 | 6% |
| Unknown | 5 | 16% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 11 | 34% |
| Agricultural and Biological Sciences | 7 | 22% |
| Chemistry | 3 | 9% |
| Pharmacology, Toxicology and Pharmaceutical Science | 1 | 3% |
| Chemical Engineering | 1 | 3% |
| Other | 4 | 13% |
| Unknown | 5 | 16% |
Attention Score in Context
This research output has an Altmetric Attention Score of 14. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 November 2023.
All research outputs
#2,379,984
of 23,810,331 outputs
Outputs from PLOS ONE
#29,916
of 203,376 outputs
Outputs of similar age
#15,160
of 165,783 outputs
Outputs of similar age from PLOS ONE
#491
of 3,956 outputs
Altmetric has tracked 23,810,331 research outputs across all sources so far. Compared to these this one has done well and is in the 89th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 203,376 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 15.5. This one has done well, scoring higher than 85% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 165,783 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 90% of its contemporaries.
We're also able to compare this research output to 3,956 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 87% of its contemporaries.