Evidence map›Paper›PMID 16269704›Full record

ArticleApplied and environmental microbiology2005

Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases.

Andrea Jesenská, Martina Pavlová, Michal Strouhal, Radka Chaloupková, Iva Tesínská, Marta Monincová, Zbynek Prokop, Milan Bartos, Ivo Pavlík, Ivan Rychlík and 3 more

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 53 citations in OpenAlex.

  1. Structural Analysis of the Ancestral Haloalkane Dehalogenase AncLinB-DmbA.International journal of molecular sciences · 2021
    Article
  2. Article
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  4. Discovery of Novel Haloalkane Dehalogenase Inhibitors.Applied and environmental microbiology · 2016
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  11. Crystallization and preliminary X-ray analysis of a novel haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  12. 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

13 authors at 3 institutions in 2 countries.

Andrea JesenskáLoschmidt Laboratories, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic. andreaj@chemi.muni.cz
Martina Pavlová
Michal Strouhal
Radka Chaloupková
Iva Tesínská
Marta Monincová
Zbynek Prokop
Milan Bartos
Ivo Pavlík
Ivan Rychlík
Petra Möbius
Yuji Nagata
Jiri Damborsky
Masaryk University · CZVeterinary Research Institute · CZTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Haloalkane dehalogenases are enzymes that catalyze the cleavage of the carbon-halogen bond by a hydrolytic mechanism. Genomes of Mycobacterium tuberculosis and M. bovis contain at least two open reading frames coding for the polypeptides showing a high sequence similarity with biochemically characterized haloalkane dehalogenases. We describe here the cloning of the haloalkane dehalogenase genes dmbA and dmbB from M. bovis 5033/66 and demonstrate the dehalogenase activity of their translation products. Both of these genes are widely distributed among species of the M. tuberculosis complex, including M. bovis, M. bovis BCG, M. africanum, M. caprae, M. microti, and M. pinnipedii, as shown by the PCR screening of 48 isolates from various hosts. DmbA and DmbB proteins were heterologously expressed in Escherichia coli and purified to homogeneity. The DmbB protein had to be expressed in a fusion with thioredoxin to obtain a soluble protein sample. The temperature optimum of DmbA and DmbB proteins determined with 1,2-dibromoethane is 45 degrees C. The melting temperature assessed by circular dichroism spectroscopy of DmbA is 47 degrees C and DmbB is 57 degrees C. The pH optimum of DmbA depends on composition of a buffer with maximal activity at 9.0. DmbB had a single pH optimum at pH 6.5. Mycobacteria are currently the only genus known to carry more than one haloalkane dehalogenase gene, although putative haloalkane dehalogenases can be inferred in more then 20 different bacterial species by comparative genomics. The evolution and distribution of haloalkane dehalogenases among mycobacteria is discussed.

Indexed as

Cloning, MolecularAnimalsBacterial ProteinsCattleEnzyme StabilityHumansHydrogen-Ion ConcentrationHydrolasesMolecular Sequence DataMycobacteriumMycobacterium bovisSequence Analysis, DNATemperatureBacterial Proteinshaloalkane dehalogenaseHydrolases

Identifiers

PMID16269704
PMCPMC1287712
OpenAlexW2168839677

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.