ArticleScientific reports2017
Insights into substrate binding of ferulic acid esterases by arabinose and methyl hydroxycinnamate esters and molecular docking.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Analysis of the Atypical Temperature Dependence and Conformational Changes During Turnover of a Lactobacillus Chlorogenic Acid Esterase.Biochemistry · 2026Article
- Diet-gut microbiome interaction and ferulic acid bioavailability: implications on neurodegenerative disorders.European journal of nutrition · 2024Review
- The Inhibitory Potential of Ferulic Acid Derivatives against the SARS-CoV-2 Main Protease: Molecular Docking, Molecular Dynamics, and ADMET Evaluation.Biomedicines · 2022Article
- Biochemical characterization of a novel feruloyl esterase from3 Biotech · 2022Article
- Regioselective chemoenzymatic syntheses of ferulate conjugates as chromogenic substrates for feruloyl esterases.Beilstein journal of organic chemistry · 2021Article
- Polyphenol-Mediated Gut Microbiota Modulation: Toward Prebiotics and Further.Frontiers in nutrition · 2021Review
- A biorefinery approach for the production of ferulic acid from agroresidues through ferulic acid esterase of lactic acid bacteria.3 Biotech · 2020Article
- Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme fromBiotechnology for biofuels · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferulic acid esterases (FAE, EC 3.1.1.73) cleave the arabinose hydroxycinnamate ester in plant hemicellulose and other related substrates. FAE are commonly categorised as type A-D based on catalytic activities towards model, short alkyl chain esters of hydroxycinnamates. However, this system correlates poorly with sequence and structural features of the enzymes. In this study, we investigated the basis of the type A categorisation of an FAE from Aspergillus niger, AnFaeA, by comparing its activity toward methyl and arabinose hydroxycinnamate esters. k
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