ArticleThe FEBS journal2022
Crystal structure of a family VIII β-lactamase fold hydrolase reveals the molecular mechanism for its broad substrate scope.
Article in The FEBS journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Bacterial family-VIII esterase displays dual activities: hydrolysis of polyester bioplastics and β-lactam antibiotics.The ISME journal · 2026Article
- Molecular war and peace: the concurrent path to antibiosis and antibiotic resistance.Frontiers in microbiology · 2026Review
- Biodegradation of Poly(ε-caprolactone): Microorganisms, Enzymes, and Mechanisms.International journal of molecular sciences · 2025Review
- Crystal Structure of EstZF172 Catalyzing Stereoselectively (ACS omega · 2025Article
- β-Lactams from the Ocean.Marine drugs · 2023Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Family VIII esterases present similarities to class C β-lactamases, which show nucleophilic serines located at the S-X-X-K motif instead of the G-X-S-X-G or G-D-S-(L) motif shown by other carboxylesterase families. Here, we report the crystal structure of a novel family VIII (subfamily VIII. I) esterase (EH
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Registered trials
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.