ArticleBiotechnology letters2024
Production of derivatives of α-terpineol by bacterial CYP102A1 enzymes.
Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Caver Web 2.0: analysis of tunnels and ligand transport in dynamic ensembles of proteins.Nucleic acids research · 2025Article
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Authors and funding
5 authors.
Funding
Abstract
The monooxygenase activity of engineered CYP102A1 on α-terpineol was investigated. CYP102A1 M850 mutant (F11Y/R47L/D68G/F81I/F87V/E143G/L188Q/E267V/H408R) showed the highest catalytic activity toward α-terpineol among the engineered mutants produced by random mutagenesis. The major product (P1) of α-terpineol, p-menth-1-ene-3,8-diol, was characterized by high-performance liquid chromatography, gas-chromatography mass spectrometry, and nuclear magnetic resonance spectroscopy. Three minor products (P2-P4) of α-terpineol were considered as 6-hydroxy-α,α,4-trimethyl-3-cyclohexene-1-methanol (P2), trans-sobrerol (P3), and carvone hydrate (P4). Optimal conditions for product formation were determined as pH 7.0 and 30 °C. Production of p-menth-1-ene-3,8-diol was 0.87 mM at 1 h. Structure modeling using PyMOL and CAVER Web 1.2 server indicated that several mutations of CYP102A1 M850 were involved in access tunnels and active sites, resulting in increased activity toward α-terpineol. The major product, p-menth-1-ene-3,8-diol, of α-terpineol was produced by engineered CYP102A1 M850 via regioselective carbon hydroxylation. The engineered CYP102A1 could be a suitable biocatalyst for producing α-terpineol derivatives.
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Registered trials
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