Evidence map›Paper›PMID 16672512›Full record

ArticleApplied and environmental microbiology2006

Isolation and biochemical characterization of two novel metagenome-derived esterases.

C Elend, C Schmeisser, C Leggewie, P Babiak, J D Carballeira, H L Steele, J-L Reymond, K-E Jaeger, W R Streit

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Class C β-Lactamases: Molecular Characteristics.Clinical microbiology reviews · 2022
    Review
  5. Article
  6. Article
  7. Emerging priorities for microbial metagenome research.Bioresource technology reports · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  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

9 authors.

C ElendMolekulare Enzymtechnologie, Universität Duisburg-Essen, Lotharstrasse 1, 47057 Duisburg, Germany.
C Schmeisser
C Leggewie
P Babiak
J D Carballeira
H L Steele
J-L Reymond
K-E Jaeger
W R Streit

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The metagenomes of uncultured microbial communities are rich sources for novel biocatalysts. In this study, esterase EstA3 was derived from a drinking water metagenome, and esterase EstCE1 was derived from a soil metagenome. Both esterases are approximately 380 amino acids in size and show similarity to beta-lactamases, indicating that they belong to family VIII of the lipases/esterases. EstA3 had a temperature optimum at 50 degrees C and a pH optimum at pH 9.0. It was remarkably active and very stable in the presence of solvents and over a wide temperature and pH range. It is active in a multimeric form and displayed a high level of activity against a wide range of substrates including one secondary ester, 7-[3-octylcarboxy-(3-hydroxy-3-methyl-butyloxy)]-coumarin, which is normally unreactive. EstCE1 was active in the monomeric form and had a temperature optimum at 47 degrees C and a pH optimum at pH 10. It exhibited the same level of stability as EstA3 over wide temperature and pH ranges and in the presence of dimethyl sulfoxide, isopropanol, and methanol. EstCE1 was highly enantioselective for (+)-menthylacetate. These enzymes display remarkable characteristics that cannot be related to the original environment from which they were derived. The high level of stability of these enzymes together with their unique substrate specificities make them highly useful for biotechnological applications.

Indexed as

Genomic LibrarySoil MicrobiologyBacterial ProteinsEnzyme StabilityEsterasesFresh WaterHydrogen-Ion ConcentrationMolecular Sequence DataSequence Analysis, DNASolventsSubstrate SpecificityTemperatureBacterial ProteinsEsterasesSolvents

Identifiers

PMID16672512
PMCPMC1472341

What OpenQuestion holds

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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.