Evidence map›Paper›PMID 21221938›Full record

ArticleJournal of microbiology (Seoul, Korea)2010

Characterization of hyperthermostable fructose-1,6-bisphosphatase from Thermococcus onnurineus NA1.

Yeol Gyun Lee, Sung Gyun Kang, Jung-Hyun Lee, Seung Il Kim, Young-Ho Chung

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Article in Journal of microbiology (Seoul, Korea), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

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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

2 citing papers in PubMed.

  1. Article
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4 · The record

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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

5 authors.

Yeol Gyun LeeDivision of Life Science, Korea Basic Science Institute, Daejeon, 305-806, Republic of Korea.
Sung Gyun Kang
Jung-Hyun Lee
Seung Il Kim
Young-Ho Chung

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To understand the physiological functions of thermostable fructose-1,6-bisphosphatase (TNA1-Fbp) from Thermococcus onnurineus NA1, its recombinant enzyme was overexpressed in Escherichia coli, purified, and the enzymatic properties were characterized. The enzyme showed maximal activity for fructose-1,6-bisphosphate at 95°C and pH 8.0 with a half-life (t (1/2)) of about 8 h. TNA1-Fbp had broad substrate specificities for fructose-1,6-bisphosphate and its analogues including fructose-1-phosphate, glucose-1-phosphate, and phosphoenolpyruvate. In addition, its enzyme activity was increased five-fold by addition of 1 mM Mg(2+), while Li(+) did not enhance enzymatic activity. TNA1-Fbp activity was inhibited by ATP, ADP, and phosphoenolpyruvate, but AMP up to 100 mM did not have any effect. TNA1-Fbp is currently defined as a class V fructose-1,6-bisphosphatase (FBPase) because it is very similar to FBPase of Thermococcus kodakaraensis KOD1 based on sequence homology. However, this enzyme shows a different range of substrate specificities. These results suggest that TNA1-Fbp can establish new criterion for class V FBPases.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateCloning, MolecularEnzyme ActivatorsEnzyme InhibitorsEscherichia coliFructose-BisphosphataseFructosephosphatesGene ExpressionGlucosephosphatesHalf-LifeHot TemperatureHydrogen-Ion ConcentrationMagnesiumPhosphoenolpyruvateRecombinant ProteinsAdenosine DiphosphateAdenosine TriphosphateEnzyme ActivatorsEnzyme Inhibitorsfructose-1-phosphateFructose-BisphosphataseFructosephosphatesglucose-1-phosphateGlucosephosphatesMagnesiumPhosphoenolpyruvateRecombinant Proteins

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Registered trials

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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.