Evidence map›Paper›PMID 9401025›Full record

ArticleJournal of bacteriology1997

Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity.

R Peist, A Koch, P Bolek, S Sewitz, T Kolbus, W Boos

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  3. Review
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  9. Article
  10. A critical examination of Escherichia coli esterase activity.The Journal of biological chemistry · 2009
    Article
  11. Article
  12. Article
  13. Crystallization and preliminary X-ray diffraction analysis of ybfF, a new esterase from Escherichia coli K12.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

R PeistDepartment of Biology, University of Konstanz, Germany.
A Koch
P Bolek
S Sewitz
T Kolbus
W Boos
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

malQ mutants of Escherichia coli lacking amylomaltase cannot grow on maltose. They express the maltose system constitutively and are sensitive to maltose when grown on another carbon source. In an attempt to isolate a multicopy suppressor that would result in growth on maltose, we transformed a malQ mutant with a gene bank of E. coli DNA which had been digested with Sau3a and cloned in pBR322. We screened the transformants on MacConkey maltose plates. A colony was isolated that appeared to be resistant to maltose and was pink on these plates, but it was still unable to grow on minimal medium with maltose as the carbon source. The plasmid was isolated, and the gene causing this phenotype was characterized. The deduced amino acid sequence of the encoded protein shows homology to that of lipases and esterases. We termed the gene aes, for acetyl esterase. Extracts of cells harboring plasmid-encoded aes under its own promoter exhibit a fivefold higher capacity to hydrolyze p-nitrophenyl acetate than do extracts of cells of plasmid-free strains. Similarly, strains harboring plasmid-encoded aes are able to grow on triacetyl glycerol (triacetin) whereas the plasmid-free strains are not. The expression of plasmid-encoded aes resulted in strong repression of the maltose transport genes in malT+ strains (10-fold reduction), but not in a malT(Con) strain which is independent of the inducer. Also, overproduction of MalT counteracted the Aes-dependent repression, indicating a direct interaction between MalT and Aes.

Indexed as

Genes, BacterialAcetylesteraseAmino Acid SequenceBacterial ProteinsBase SequenceBiological TransportCytoplasmEscherichia coliGene Expression Regulation, BacterialMaltoseMolecular Sequence DataPlasmidsSequence Homology, Amino AcidAcetylesteraseBacterial ProteinsMaltose

Identifiers

PMID9401025
PMCPMC179729
OpenAlexW2115412292

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.