Related Experiment Video
Updated: Jun 12, 2025
13:35
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
210
Structural insight into sugar-binding modes of microbial ß-amylase
1Department of Natural Science, Graduate School of Technology, Industrial and Social Science, Tokushima University, 2-1 Minamijosanjimacho, Tokushima, Tokushima, 770-8506, Japan.
Biochemical and Biophysical Research Communications
|September 17, 2024
Summary
Bacillus cereus β-amylase (BCB) crystal structure reveals new sugar-binding sites crucial for raw starch degradation. This detailed information aids protein engineering for enhanced enzyme activity in food processing.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- ß-Amylase is vital in the food industry for starch processing.
- Protein engineering can enhance enzyme activity for improved food processing efficiency.
Purpose of the Study:
- To determine the crystal structure of Bacillus cereus β-amylase (BCB) complexed with maltose.
- To provide detailed structural insights for rational protein engineering of BCB.
Main Methods:
- X-ray crystallography
- Molecular replacement
- Anisotropic temperature factor refinement
- High-resolution structure determination (1.26 Å)
Main Results:
- The crystal structure of BCB complexed with six maltose and one glucose molecule was determined.
- Three novel sugar-binding sites were identified on the enzyme surface, potentially enhancing raw starch degradation.
- Two maltose molecules were observed bound in tandem within the active site.
- A distorted α-glucose conformation at subsite -1 suggests it is not directly involved in catalysis.
Conclusions:
- The high-resolution structure provides critical insights into BCB's mechanism and substrate binding.
- The newly identified surface-binding sites offer targets for protein engineering to improve enzyme function.
- These findings facilitate the development of enhanced microbial ß-amylase enzymes for industrial applications.
Keywords:
Bacillus cereusDistorted sugar formationNovel sugar-binding sitesRaw-starch digestionβ-amylaseMore Related Videos
Related Concept Videos
00:49Ligand Binding and Linkage
4.8K
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...
4.8K
03:25Chemistry of Carbohydrates
71.9K
Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
71.9K
01:19Allosteric Proteins-ATCase
5.7K
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...
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...
5.7K
02:15Protein and Protein Structure
79.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.0K
01:24Oligosaccharide Assembly
2.8K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.8K
02:18Fischer Projections
13.1K
Learning to draw Fischer projections of molecules and understanding their relevance plays a crucial role in the visual depiction of organic molecules. A Fischer projection is a two-dimensional projection on a planar surface to simplify the three-dimensional wedge–dash representation of molecules. This is especially helpful in the case of molecules with multiple chiral centers that can be difficult to draw. Here, all the bonds of interest are represented as horizontal or vertical lines.
13.1K