ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2024
Flexible active-site loops fine-tune substrate specificity of hyperthermophilic metallo-oxidases.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2024. 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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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- FireProtDB 2.0: large-scale manually curated database of the protein stability data.Nucleic acids research · 2026Article
- Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol.Angewandte Chemie (International ed. in English) · 2025Article
- Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025Article
- Enzyme-Modified Microelectrode for Simultaneous Local Measurements of OAnalytical chemistry · 2024Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Hyperthermophilic ('superheat-loving') archaea found in high-temperature environments such as Pyrobaculum aerophilum contain multicopper oxidases (MCOs) with remarkable efficiency for oxidizing cuprous and ferrous ions. In this work, directed evolution was used to expand the substrate specificity of P. aerophilum McoP for organic substrates. Six rounds of error-prone PCR and DNA shuffling followed by high-throughput screening lead to the identification of a hit variant with a 220-fold increased efficiency (k
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Registered trials
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