Evidence map›Paper›PMID 15659684›Full record

ArticleJournal of bacteriology2005

Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli.

Kwok Ki Ho, Henry Weiner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 76 citations in OpenAlex.

  1. Nutrient control enables metabolic reconstruction ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
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  6. Zymomonas mobilis ZM4 Utilizes an NADPJournal of bacteriology · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Metabolic Engineering ofFrontiers in bioengineering and biotechnology · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Kwok Ki HoBiochemistry Department, Purdue University, West Lafayette, IN 47904-2063, USA.
Henry Weiner
Purdue University West Lafayette · US

Funding

IN VIVO AND VITRO REGULATION OF ACETALDEHYDE METABOLISMR01AA005812 · NIAAA · PURDUE UNIVERSITY WEST LAFAYETTE · PI WEINER, HENRY · 1985 to 2007
$2.0M
ENZYMOLOGY/MOLECULAR BIOLOGY OF ALDEHYDE DEHYDROGENASER37AA005812 · NIAAA · PURDUE UNIVERSITY WEST LAFAYETTE · PI WEINER, HENRY · 1989 to 1996
–
NIAAA NIH HHS AA05812NIAAA NIH HHS R01 AA005812NIAAA NIH HHS R37 AA005812
6 · The paper itself

Abstract

An aldehyde dehydrogenase was detected in crude cell extracts of Escherichia coli DH5alpha. Growth studies indicated that the aldehyde dehydrogenase activity was growth phase dependent and increased in cells grown with ethanol. The N-terminal amino acid sequence of the purified enzyme identified the latter as an aldehyde dehydrogenase encoded by aldB, which was thought to play a role in the removal of aldehydes and alcohols in cells that were under stress. The purified enzyme showed an estimated molecular mass of 220 +/- 8 kDa, consisting of four identical subunits, and preferred to use NADP and acetaldehyde. MgCl2 increased the activity of the NADP-dependent enzyme with various substrates. A comparison of the effect of Mg2+ ions on the bacterial enzyme with the effect of Mg2+ ions on human liver mitochondrial aldehyde dehydrogenase revealed that the bacterial enzyme shared kinetic properties with the mammalian enzyme. An R197E mutant of the bacterial enzyme appeared to retain very little NADP-dependent activity on acetaldehyde.

Indexed as

Aldehyde DehydrogenaseAmino Acid SequenceBase SequenceBinding SitesChromatography, AffinityChromatography, Ion ExchangeDNA PrimersEscherichia coliGenes, BacterialHumansKineticsMalate DehydrogenaseModels, MolecularMolecular Sequence DataProtein ConformationSequence AlignmentAldehyde DehydrogenaseDNA PrimersMalate Dehydrogenase

Identifiers

PMID15659684
PMCPMC545698
OpenAlexW2143734654

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.