Evidence map›Paper›PMID 24429289›Full record

ArticleThe Journal of biological chemistry2014

Characterization of a novel subtilisin-like protease myroicolsin from deep sea bacterium Myroides profundi D25 and molecular insight into its collagenolytic mechanism.

Li-Yuan Ran, Hai-Nan Su, Ming-Yang Zhou, Lei Wang, Xiu-Lan Chen, Bin-Bin Xie, Xiao-Yan Song, Mei Shi, Qi-Long Qin, Xiuhua Pang and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Thermostable Proteases fromMicroorganisms · 2025
    Review
  3. Thermostable Bacterial Collagenolytic Proteases: A Review.Journal of microbiology and biotechnology · 2024
    Review
  4. Article
  5. Article
  6. Microbial proteases and their applications.Frontiers in microbiology · 2023
    Review
  7. Sec-Dependent Secretion of Subtilase SptE inApplied and environmental microbiology · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. A Novel Gelatinase from MarineMarine drugs · 2022
    Article
  13. Taxonomic and Enzymatic Characterization ofFrontiers in microbiology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Genome Sequencing ofFrontiers in microbiology · 2019
    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

13 authors at 2 institutions in 1 country.

Li-Yuan RanFrom the State Key Laboratory of Microbial Technology.
Hai-Nan Su
Ming-Yang Zhou
Lei Wang
Xiu-Lan Chen
Bin-Bin Xie
Xiao-Yan Song
Mei Shi
Qi-Long Qin
Xiuhua Pang
Bai-Cheng Zhou
Yu-Zhong Zhang
Xi-Ying Zhang
Shandong University · CNState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagen is an insoluble protein that widely distributes in the extracellular matrix of marine animals. Collagen degradation is an important step in the marine nitrogen cycle. However, the mechanism of marine collagen degradation is still largely unknown. Here, a novel subtilisin-like collagenolytic protease, myroicolsin, which is secreted by the deep sea bacterium Myroides profundi D25, was purified and characterized, and its collagenolytic mechanism was studied. Myroicolsin displays low identity (<30%) to previously characterized subtilisin-like proteases, and it contains a novel domain structure. Protein truncation indicated that the Pro secretion system C-terminal sorting domain in the precursor protein is involved in the cleavage of the N-propeptide, and the linker is required for protein folding during myroicolsin maturation. The C-terminal β-jelly roll domain did not bind insoluble collagen fiber, suggesting that myroicolsin may degrade collagen without the assistance of a collagen-binding domain. Myroicolsin had broad specificity for various collagens, especially fish-insoluble collagen. The favored residue at the P1 site was basic arginine. Scanning electron microscopy and atomic force microscopy, together with biochemical analyses, confirmed that collagen fiber degradation by myroicolsin begins with the hydrolysis of proteoglycans and telopeptides in collagen fibers and fibrils. Myroicolsin showed strikingly different cleavage patterns between native and denatured collagens. A collagen degradation model of myroicolsin was proposed based on our results. Our study provides molecular insight into the collagen degradation mechanism and structural characterization of a subtilisin-like collagenolytic protease secreted by a deep sea bacterium, shedding light on the degradation mechanism of deep sea sedimentary organic nitrogen.

Indexed as

Water MicrobiologyBacterial ProteinsBase SequenceCollagenFlavobacteriaceaeMolecular Sequence DataSeawaterSubtilisinBacterial ProteinsCollagenSubtilisinBacteriaBiodegradationCollagenCollagenolytic MechanismDeep Sea SedimentEnzyme MechanismsNitrogen CyclingSerine ProteaseStructural CharacteristicsSubtilisin-like Protease

Identifiers

PMID24429289
PMCPMC3937671
OpenAlexW2072015196

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.