ArticleScientific reports2016
Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed.
- First experimentally characterised Proteus phage endolysins have distinct metal cofactor dependencies.Applied microbiology and biotechnology · 2026Article
- Future Perspective and Technological Innovation in Cheese Making Using Artichoke (Foods (Basel, Switzerland) · 2023Review
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Plant Milk-Clotting Enzymes for Cheesemaking.Foods (Basel, Switzerland) · 2022Review
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Authors and funding
12 authors.
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Abstract
A current metagenomics focus is to interpret and transform collected genomic data into biological information. By combining structural, functional and genomic data we have assessed a novel bacterial protein selected from a carbohydrate-related activity screen in a microbial metagenomic library from Capra hircus (domestic goat) gut. This uncharacterized protein was predicted as a bacterial cell wall-modifying enzyme (CWME) and shown to contain four domains: an N-terminal, a cysteine protease, a peptidoglycan-binding and an SH3 bacterial domain. We successfully cloned, expressed and purified this putative cysteine protease (PCP), which presented autoproteolytic activity and inhibition by protease inhibitors. We observed cell wall hydrolytic activity and ampicillin binding capacity, a characteristic of most bacterial CWME. Fluorimetric binding analysis yielded a K
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