ArticleScientific reports2018
Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Advances in amidases and urethanases as depolymerization biocatalysts.Nature chemical biology · 2026Review
- Trylons: Polyamide Surrogate Substrates Enable High-Throughput Screening of Nylon-Degrading Enzymes.Chembiochem : a European journal of chemical biology · 2026Article
- Challenges and opportunities in the enzymatic recycling of nylons.Nature chemical biology · 2026Review
- Structural and oligomeric characterization of substrate- and product-selective nylon hydrolases.bioRxiv : the preprint server for biology · 2026Article
- The biochemical mechanisms of plastic biodegradation.FEMS microbiology reviews · 2024Review
- Identification and characterization of substrate- and product-selective nylon hydrolases.bioRxiv : the preprint server for biology · 2024Article
- Natural diversity screening, assay development, and characterization of nylon-6 enzymatic depolymerization.Nature communications · 2024Article
- Characterization and engineering of branched short-chain dicarboxylate metabolism in Pseudomonas reveals resistance to fungal 2-hydroxyparaconate.Metabolic engineering · 2023Article
- On the Role of Platelet-Generated Amyloid Beta Peptides in Certain Amyloidosis Health Complications.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
Nylon hydrolase (NylC) is initially expressed as an inactive precursor (36 kDa). The precursor is cleaved autocatalytically at Asn266/Thr267 to generate an active enzyme composed of an α subunit (27 kDa) and a β subunit (9 kDa). Four αβ heterodimers (molecules A-D) form a doughnut-shaped quaternary structure. In this study, the thermostability of the parental NylC was altered by amino acid substitutions located at the A/D interface (D122G/H130Y/D36A/L137A) or the A/B interface (E263Q) and spanned a range of 47 °C. Considering structural, biophysical, and biochemical analyses, we discuss the structural basis of the stability of nylon hydrolase. From the analytical centrifugation data obtained regarding the various mutant enzymes, we conclude that the assembly of the monomeric units is dynamically altered by the mutations. Finally, we propose a model that can predict whether the fate of the nascent polypeptide will be correct subunit assembly, inappropriate protein-protein interactions causing aggregation, or intracellular degradation of the polypeptide.
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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.