Evidence map›Paper›PMID 9726890›Full record

ArticleApplied and environmental microbiology1998

Genetic characterization and physiological role of endopeptidase O from Lactobacillus helveticus CNRZ32.

Y S Chen, J L Steele

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

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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.

Y S ChenDepartment of Food Science, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
J L Steele

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A previously identified insert expressing an endopeptidase from a Lactobacillus helveticus CNRZ32 genomic library was characterized. Nucleotide sequence analysis revealed an open reading frame of 1,941 bp encoding a putative protein of 71.2 kDa which contained a zinc-protease motif. Protein homology searches revealed that this enzyme has 40% similarity with endopeptidase O (PepO) from Lactococcus lactis P8-2-47. Northern hybridization revealed that pepO is monocistronic and is expressed throughout the growth phase. CNRZ32 derivatives lacking PepO activity were constructed via gene replacement. Enzyme assays revealed that the PepO mutant had significantly reduced endopeptidase activity when compared to CNRZ32 with two of the three substrates examined. Growth studies indicated that PepO has no detectable effect on growth rate or acid production by Lactobacillus helveticus CNRZ32 in amino acid defined or skim milk medium.

Indexed as

Bacterial ProteinsAmino Acid SequenceAnimalsBase SequenceBlotting, SouthernCloning, MolecularCulture MediaDNA, BacterialDNA Transposable ElementsGene DeletionLactobacillusMetalloendopeptidasesMilkMolecular Sequence DataMutagenesis, InsertionalPlasmidsBacterial ProteinsCulture MediaDNA, BacterialDNA Transposable ElementsMetalloendopeptidasesoligopeptidase PepORNA, Messenger

Identifiers

PMID9726890
PMCPMC106740

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.