Evidence map›Paper›PMID 18782759›Full record

ArticleThe Journal of biological chemistry2008

The pathway via D-galacturonate/L-galactonate is significant for ascorbate biosynthesis in Euglena gracilis: identification and functional characterization of aldonolactonase.

Takahiro Ishikawa, Hitoshi Nishikawa, Youngshun Gao, Yoshihiro Sawa, Hitoshi Shibata, Yukinori Yabuta, Takanori Maruta, Shigeru Shigeoka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 68 citations in OpenAlex.

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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

8 authors at 4 institutions in 1 country.

Takahiro IshikawaFaculty of Life and Environmental Science, Shimane University, Matsue, Shimane 690-8504, Japan. ishikawa@life.shimane-u.ac.jp
Hitoshi Nishikawa
Youngshun Gao
Yoshihiro Sawa
Hitoshi Shibata
Yukinori Yabuta
Takanori Maruta
Shigeru Shigeoka
Shimane University · JPKindai University · JPTottori University · JPUniversity of Shimane · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously proposed that Euglena gracilis possesses a pathway for the production of ascorbate (AsA) through d-galacturonate/L-galactonate as representative intermediates ( Shigeoka, S., Nakano, Y., and Kitaoka, S. (1979) J. Nutr. Sci. Vitaminol. 25, 299-307 ). However, genetic evidence proving that the pathway exists has not been obtained yet. We report here the identification of a gene encoding aldonolactonase, which catalyzes a penultimate step of the biosynthesis of AsA in Euglena. By a BLAST search, we identified one candidate for the enzyme having significant sequence identity with rat gluconolactonase, a key enzyme for the production of AsA via d-glucuronate in animals. The purified recombinant aldonolactonase expressed in Escherichia coli catalyzed the reversible reaction of L-galactonate and L-galactono-1,4-lactone with zinc ion as a cofactor. The apparent K(m) values for L-galactonate and L-galactono-1,4-lactone were 1.55 +/- 0.3 and 1.67 +/- 0.39 mm, respectively. The cell growth of Euglena was arrested by silencing the expression of aldonolactonase through RNA interference and then restored to the normal state by supplementation with L-galactono-1,4-lactone. Euglena cells accumulated more AsA on supplementation with d-galacturonate than d-glucuronate. The present results indicate that aldonolactonase is significant for the biosynthesis of AsA in Euglena cells, which predominantly utilize the pathwayviad-galacturonate/L-galactonate. The identification of aldonolactonase provides the first insight into the biosynthesis of AsA via uronic acids as the intermediate in photosynthetic algae including Euglena.

Indexed as

Algal ProteinsAmino Acid SequenceAnimalsAscorbic AcidCarboxylic Ester HydrolasesEscherichia coliEuglena gracilisHexuronic AcidsMolecular Sequence DataProtozoan ProteinsRatsRecombinant ProteinsSugar AcidsAlgal ProteinsAscorbic AcidCarboxylic Ester Hydrolasesgalactonic acidgalacturonic acidgluconolactonaseHexuronic AcidsProtozoan ProteinsRecombinant ProteinsSugar Acids

Identifiers

PMID18782759
PMCPMC2662179
OpenAlexW2015002292

What OpenQuestion holds

Textmetadata
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.