Related Experiment Video
Updated: Jun 20, 2026
06:51
High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
Published on: September 20, 2016
Comparative characterization of commercially important xylanase enzymes
Neelima Arora1, Amit Kumar Banerjee, Srilaxmi Mutyala
1Bioinformatics Group, Biology Division, Indian Institute of Chemical Technology, Hyderabad-500007, A.P., India.
Bioinformation
|September 18, 2009
Summary
This study used bioinformatics to analyze xylanase enzymes, revealing common active site residues like Asn72. Understanding xylanase structure is key for industrial applications, particularly in the paper industry.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Xylanases are industrially significant enzymes with broad applications, especially in the paper industry.
- Understanding the structure and function of diverse xylanases is crucial for optimizing their industrial use.
Purpose of the Study:
- To explore the properties and structure of xylanases using bioinformatics and molecular modeling.
- To characterize xylanases through prediction of motifs, disulfide bridges, and secondary structures.
Main Methods:
- Bioinformatics and molecular modeling approaches were employed.
- Physico-chemical properties, motifs, disulfide bridges, and secondary structures were predicted.
- Three-dimensional structures were constructed and validated; catalytic sites were analyzed.
Main Results:
- Predicted physico-chemical properties and functional characteristics of xylanases.
- Constructed and validated three-dimensional protein structures.
- Identified Asn72 as a common residue in the active sites of proteins P35809 and Q12603.
Conclusions:
- Bioinformatics and molecular modeling provide valuable insights into xylanase structure-function relationships.
- The identification of conserved residues like Asn72 can guide enzyme engineering for industrial applications.
Related Concept Videos
01:30Enzyme Inhibition
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
01:19Enzyme Kinetics
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...