Evidence map›Paper›PMID 40691222›Full record

ArticleScientific reports2025

Substrate profiling of marine-derived thermotolerant cysteine protease reveals unique cleavage preferences for industrial applications.

Victoria Røyseth, Brianna M Hurysz, Hasan Arsın, Julia M Vazquez, Anna-Karina Kaczorowska, Anita-Elin Fedøy, Daria Biernacka, Sebastian Dorawa, Tadeusz Kaczorowski, Runar Stokke and 2 more

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Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
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0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Victoria Røyseth *Department of Biological Sciences, Center for Deep Sea Research, University of Bergen, Bergen, Norway.
Brianna M Hurysz *Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, USA.
Hasan ArsınDepartment of Biological Sciences, Center for Deep Sea Research, University of Bergen, Bergen, Norway.
Julia M VazquezSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, USA.
Anna-Karina KaczorowskaCollection of Plasmids and Microorganisms | KPD, Faculty of Biology, University of Gdańsk, Gdańsk, Poland.
Anita-Elin FedøyDepartment of Biological Sciences, Center for Deep Sea Research, University of Bergen, Bergen, Norway.
Daria BiernackaCollection of Plasmids and Microorganisms | KPD, Faculty of Biology, University of Gdańsk, Gdańsk, Poland.
Sebastian DorawaLaboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdańsk, Gdańsk, Poland.
Tadeusz KaczorowskiLaboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdańsk, Gdańsk, Poland.
Runar StokkeDepartment of Biological Sciences, Center for Deep Sea Research, University of Bergen, Bergen, Norway.
Anthony J O'DonoghueSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, USA. ajodonoghue@health.ucsd.edu.
Ida Helene SteenDepartment of Biological Sciences, Center for Deep Sea Research, University of Bergen, Bergen, Norway. ida.steen@uib.no.

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Microbiome Driven Proteolysis as a Contributing Factor to Severity of Ulcerative Colitis Disease ActivityR01DK131005 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GONZALEZ, DAVID J · 2022 to 2024
$1.6M
NIDDK NIH HHS R01 DK131005NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

Due to their industrial importance, new proteases are constantly being sourced from the marine environment. However, their substrate specificities remain insufficiently studied, restricting the evaluation of their potential applications. Here, we applied multiplex substrate profiling by mass spectrometry (MSP-MS) to globupain, a marine thermotolerant clostripain-like protease and show that it has a novel substrate specificity. Globupain is an endopeptidase with a preference for cleavage of substrates on the C-terminal side of norleucine (Nle), Leu, Asn, Arg and Lys. While it can hydrolyze gelatin and collagen, its reaction rate is lower than that of papain, a commercial cysteine protease. The precise knowledge of substrate specificity of globupain led to the discovery that the calpain inhibitors MG101 and leupeptin inactivate globupain activity with IC

Indexed as

Aquatic OrganismsCysteine ProteasesGelatinLeupeptinsSubstrate SpecificityCysteine ProteasesGelatinLeupeptinsClostripainGlobupainHydrothermal ventsMarine bioprospectingMarine cysteine proteaseMultiplex substrate profiling by mass spectrometry

Identifiers

PMID40691222
PMCPMC12280095

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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.