Related Experiment Video
Updated: Jun 8, 2026

08:59
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Combining substrate specificity analysis with support vector classifiers reveals feruloyl esterase as a
Roberto Olivares-Hernández1, Hampus Sunner, Jens C Frisvad
1Department of Chemical and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden.
Plos One
|September 30, 2010
Summary
Enzyme activity profiles of feruloyl esterases (FAEs) can accurately predict fungal taxonomy. This study demonstrates FAE substrate specificity as a novel tool for classifying Ascomycota species, aiding in understanding fungal evolution and adaptation.
Area of Science:
- Mycology
- Enzymology
- Evolutionary Biology
Background:
- Fungal evolution into diverse ecological niches is poorly understood.
- Enzyme evolution is critical for species adaptation to new environments.
- Feruloyl esterases (FAEs) hydrolyze ester bonds in plant cell walls, with diverse substrate specificities.
Purpose of the Study:
- To develop a novel predictive tool for Ascomycota taxonomic classification using FAE activity.
- To evaluate the relative activity of FAEs against various model substrates.
- To correlate FAE substrate specificities with fungal phylogeny.
Main Methods:
- Cultivation of 34 Ascomycota strains to generate FAE substrate specificity data.
- Analysis of enzyme cocktails against 10 substituted cinnamate and phenylalkanoate methyl esters.
- Application of unsupervised and supervised learning models (linear and non-linear) for taxonomic prediction.
Main Results:
- Unsupervised clustering of FAE substrate specificity data.
- Supervised models achieved high accuracy in predicting taxonomic Class (~86%), Order (~88%), and Family (~88%).
- FAE activity profiles effectively classified the 34 Ascomycota strains.
Conclusions:
- FAEs are phylogenetically informative proteins, as indicated by their substrate specificities.
- FAE substrate specificity provides a reliable method for fungal taxonomic classification.
- This approach represents a significant advancement in predicting FAE functions and fungal taxonomy.
More Related Videos
Related Concept Videos
Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Ligand Binding and Linkage
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Families
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key locations, protein...

