ArticlePloS one2018
Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 29 citations in OpenAlex.
- Elucidating the catalytic mechanism of a previously undescribed carbohydrate esterase family 7 acetyl xylan esterase (LaCE7A).The FEBS journal · 2026Article
- Deacetylation of β-Mannans by Two Complementary Carbohydrate Esterases from the Human Gut MicrobeBiochemistry · 2026Article
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- Feruloyl Esterase (International journal of molecular sciences · 2023Article
- Biochemical characterization of an acetylesterase fromFrontiers in microbiology · 2023Article
- Recombinant acetylxylan esterase of Halalkalibacterium halodurans NAH-Egypt: molecular and biochemical study.AMB Express · 2022Article
- Characterisation of a Novel Acetyl Xylan Esterase (BaAXE) Screened from the Gut Microbiota of the Common Black Slug (Molecules (Basel, Switzerland) · 2022Article
- Article
- Production, purification, and process optimization of intracellular pigment from novel psychrotolerant Paenibacillus sp. BPW19.Biotechnology reports (Amsterdam, Netherlands) · 2021Article
- Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 fromJournal of microbiology and biotechnology · 2020Article
- Characterization and Immobilization of a Novel SGNH Family Esterase (International journal of molecular sciences · 2019Article
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Authors and funding
10 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cold-active acetyl xylan esterases allow for reduced bioreactor heating costs in bioenergy production. Here, we isolated and characterized a cold-active acetyl xylan esterase (PbAcE) from the psychrophilic soil microbe Paenibacillus sp. R4. The enzyme hydrolyzes glucose penta-acetate and xylan acetate, reversibly producing acetyl xylan from xylan, and it shows higher activity at 4°C than at 25°C. We solved the crystal structure of PbAcE at 2.1-Å resolution to investigate its active site and the reason for its low-temperature activity. Structural analysis showed that PbAcE forms a hexamer with a central substrate binding tunnel, and the inter-subunit interactions are relatively weak compared with those of its mesophilic and thermophilic homologs. PbAcE also has a shorter loop and different residue composition in the β4-α3 and β5-α4 regions near the substrate binding site. Flexible subunit movements and different active site loop conformations may enable the strong low-temperature activity and broad substrate specificity of PbAcE. In addition, PbAcE was found to have strong activity against antibiotic compound substrates, such as cefotaxime and 7-amino cephalosporanic acid (7-ACA). In conclusion, the PbAcE structure and our biochemical results provide the first example of a cold-active acetyl xylan esterase and a starting template for structure-based protein engineering.
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