Evidence map›Paper›PMID 12571009›Full record

ArticleApplied and environmental microbiology2003

Characterization of chitinase genes from an alkaliphilic actinomycete, Nocardiopsis prasina OPC-131.

Hiroshi Tsujibo, Takahiro Kubota, Mitsugu Yamamoto, Katsushiro Miyamoto, Yoshihiko Inamori

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2003. 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
0.9field-weighted citation impact, top 27% 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, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. AIMS microbiology · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cloning and characterization of a chitinase fromBiotechnology reports (Amsterdam, Netherlands) · 2018
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. An Alternative Bacterial Expression System UsingIranian journal of biotechnology · 2015
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Bacterial chitin utilisation at extremely haloalkaline conditions.Extremophiles : life under extreme conditions · 2012
    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

5 authors at 1 institution in 1 country.

Hiroshi TsujiboDepartment of Microbiology, Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka 569-1094, Japan. tsujibo@gly.oups.ac.jp
Takahiro Kubota
Mitsugu Yamamoto
Katsushiro Miyamoto
Yoshihiko Inamori
Osaka University of Pharmaceutical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An alkaliphilic actinomycete, Nocardiopsis prasina OPC-131, secretes chitinases, ChiA, ChiB, and ChiB Delta, in the presence of chitin. The genes encoding ChiA and ChiB were cloned and sequenced. The open reading frame (ORF) of chiA encoded a protein of 336 amino acids with a calculated molecular mass of 35,257 Da. ChiA consisted of only a catalytic domain and showed a significant homology with family 18 chitinases. The chiB ORF encoded a protein of 296 amino acids with a calculated molecular mass of 31,500 Da. ChiB is a modular enzyme consisting of a chitin-binding domain type 3 (ChtBD type 3) and a catalytic domain. The catalytic domain of ChiB showed significant similarity to Streptomyces family 19 chitinases. ChiB Delta was the truncated form of ChiB lacking ChtBD type 3. Expression plasmids coding for ChiA, ChiB, and ChiB Delta were constructed to investigate the biochemical properties of these recombinant proteins. These enzymes showed pHs and temperature optima similar to those of native enzymes. ChiB showed more efficient hydrolysis of chitin and stronger antifungal activity than ChiB Delta, indicating that the ChtBD type 3 of ChiB plays an important role in the efficient hydrolysis of chitin and in antifungal activity. Furthermore, the finding of family 19 chitinase in N. prasina OPC-131 suggests that family 19 chitinases are distributed widely in actinomycetes other than the genus Streptomyces.

Indexed as

ActinomycetalesAmino Acid SequenceBacterial ProteinsBinding SitesChitinChitinasesCloning, MolecularGenes, BacterialHydrogen-Ion ConcentrationMolecular Sequence DataPlant ProteinsRecombinant ProteinsSequence Analysis, DNABacterial ProteinsChitinchitinase ChiAChitinasesPlant ProteinsPLC-B protein, Phytolacca americanaRecombinant Proteins

Identifiers

PMID12571009
PMCPMC143619
OpenAlexW2121848676

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.