ArticleNature chemical biology2014
Revealing the hidden functional diversity of an enzyme family.
Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 126 citations in OpenAlex.
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- ASMC: investigating the amino acid diversity of enzyme active sites.Bioinformatics (Oxford, England) · 2025Article
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- Self-supervised domain adaptation of protein language model based solely on positive enzyme-reaction pairs.Computational and structural biotechnology journal · 2025Article
- An aldolase-dependent phloroglucinol degradation pathway inApplied and environmental microbiology · 2024Article
- Descriptor-augmented machine learning for enzyme-chemical interaction predictions.Synthetic and systems biotechnology · 2024Article
- Back to the Future of Metabolism-Advances in the Discovery and Characterization of Unknown Biocatalytic Functions and Pathways.Life (Basel, Switzerland) · 2024Review
- Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex.Nature communications · 2023Article
- Host macrocyclic acylcarnitines mediate symbiotic interactions between frogs and their skin microbiome.iScience · 2023Article
- Anaerobic phloroglucinol degradation bymBio · 2023Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
21 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Millions of protein database entries are not assigned reliable functions, preventing the full understanding of chemical diversity in living organisms. Here, we describe an integrated strategy for the discovery of various enzymatic activities catalyzed within protein families of unknown or little known function. This approach relies on the definition of a generic reaction conserved within the family, high-throughput enzymatic screening on representatives, structural and modeling investigations and analysis of genomic and metabolic context. As a proof of principle, we investigated the DUF849 Pfam family and unearthed 14 potential new enzymatic activities, leading to the designation of these proteins as β-keto acid cleavage enzymes. We propose an in vivo role for four enzymatic activities and suggest key residues for guiding further functional annotation. Our results show that the functional diversity within a family may be largely underestimated. The extension of this strategy to other families will improve our knowledge of the enzymatic landscape.
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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.