↓ Skip to main content

Identification and Biochemical Characterization of the Serine Biosynthetic Enzyme 3-Phosphoglycerate Dehydrogenase in Marchantia polymorpha

Overview of attention for article published in Frontiers in Plant Science, July 2018
Altmetric Badge

About this Attention Score

  • Average Attention Score compared to outputs of the same age
  • Above-average Attention Score compared to outputs of the same age and source (52nd percentile)

Mentioned by

twitter
3 X users

Citations

dimensions_citation
12 Dimensions

Readers on

mendeley
17 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Identification and Biochemical Characterization of the Serine Biosynthetic Enzyme 3-Phosphoglycerate Dehydrogenase in Marchantia polymorpha
Published in
Frontiers in Plant Science, July 2018
DOI 10.3389/fpls.2018.00956
Pubmed ID
Authors

Hiromichi Akashi, Eiji Okamura, Ryuichi Nishihama, Takayuki Kohchi, Masami Y. Hirai

Abstract

L-serine is an important molecule in all living organisms, and thus its biosynthesis is considered to be regulated according to demand. 3-Phosphoglycerate dehydrogenase (PGDH), the first committed enzyme of the phosphorylated pathway of L-serine biosynthesis, is regulated by negative feedback from L-serine in bacteria. In the case of the vascular plant Arabidopsis thaliana, two PGDH isozymes out of three are inhibited by L-serine and activated by L-alanine, L-valine, L-methionine, L-homoserine, and L-homocysteine, suggesting a more complicated regulatory mechanism of L-serine biosynthesis in A. thaliana than in bacteria. However, it remains to be clarified whether the activation mechanism of PGDH by amino acids is conserved in land plants. In this study, we identified the sole isozyme of PGDH in the liverwort Marchantia polymorpha (MpPGDH) and elucidated its biochemical characteristics. MpPGDH cDNA encodes a 65.6 kDa protein that contains a putative transit peptide for chloroplast localization. MpPGDH shares 75-80% identity with A. thaliana isozymes and forms a homotetramer in vitro. Recombinant MpPGDH exhibited an optimal pH of 9.0, apparent Michaelis constants of 0.49 ± 0.04 and 0.096 ± 0.010 mM for 3-PGA and NAD+, respectively, and apparent maximum velocity of 5.65 ± 0.10 μmol⋅min-1⋅mg-1, similar to those of A. thaliana isozymes. Phosphate ions were found to stabilize MpPGDH, suggesting that phosphate ions are also a crucial factor in the regulation of serine biosynthesis via the phosphorylated pathway in Marchantia polymorpha. MpPGDH was inhibited by L-serine in a cooperative manner and was activated by L-alanine, L-valine, L-methionine, L-homoserine, and L-homocysteine to a lesser extent than it is in A. thaliana. The results suggest that an ancestral PGDH of land plants was inhibited byL-serine and slightly activated by five other amino acids.

X Demographics

X Demographics

The data shown below were collected from the profiles of 3 X users who shared this research output. Click here to find out more about how the information was compiled.
As of 1 July 2024, you may notice a temporary increase in the numbers of X profiles with Unknown location. Click here to learn more.
Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 17 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 17 100%

Demographic breakdown

Readers by professional status Count As %
Student > Doctoral Student 3 18%
Other 3 18%
Student > Bachelor 2 12%
Student > Master 1 6%
Professor 1 6%
Other 3 18%
Unknown 4 24%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 7 41%
Agricultural and Biological Sciences 3 18%
Unknown 7 41%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. 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 19 August 2018.
All research outputs
#14,356,675
of 23,096,849 outputs
Outputs from Frontiers in Plant Science
#8,065
of 20,713 outputs
Outputs of similar age
#183,888
of 326,757 outputs
Outputs of similar age from Frontiers in Plant Science
#224
of 484 outputs
Altmetric has tracked 23,096,849 research outputs across all sources so far. This one is in the 37th percentile – i.e., 37% of other outputs scored the same or lower than it.
So far Altmetric has tracked 20,713 research outputs from this source. They receive a mean Attention Score of 3.9. This one has gotten more attention than average, scoring higher than 59% 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 326,757 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 43rd percentile – i.e., 43% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 484 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 52% of its contemporaries.