What enzyme breaks down carbohydrates

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Enzymes Responsible for Carbohydrate Breakdown

Glycoside Hydrolases: Key Enzymes in Carbohydrate Degradation

Glycoside hydrolases (GHs) are the primary enzymes responsible for breaking down carbohydrates. These enzymes catalyze the hydrolysis of glycosidic bonds within complex carbohydrates, converting them into simpler sugars. GHs are highly diverse and are classified into numerous families based on their sequence and structural characteristics 124. The Carbohydrate-Active Enzymes (CAZy) database, a comprehensive resource for information on these enzymes, lists 113 different families of glycoside hydrolases, reflecting their vast diversity and specificity .

Polysaccharide Lyases and Carbohydrate Esterases: Supporting Roles

In addition to glycoside hydrolases, other enzymes such as polysaccharide lyases and carbohydrate esterases also play crucial roles in carbohydrate breakdown. Polysaccharide lyases cleave glycosidic bonds through a mechanism that does not involve hydrolysis, while carbohydrate esterases remove ester groups from carbohydrates, facilitating further degradation by other enzymes 1410. These enzymes are essential for the complete breakdown of complex carbohydrates into their constituent sugars.

Structural and Functional Insights

Recent advances in structural biology have provided significant insights into the mechanisms of carbohydrate-active enzymes. Glycoside hydrolases, for instance, exhibit a wide variety of structural scaffolds, which are crucial for their catalytic efficiency and substrate specificity 67. Understanding these structures helps in elucidating the reaction mechanisms and in designing inhibitors that can modulate enzyme activity for therapeutic purposes .

Evolutionary and Mechanistic Perspectives

The evolutionary relationships among carbohydrate-active enzymes are reflected in their structural features rather than their substrate specificity. This evolutionary perspective helps in understanding the mechanistic properties of these enzymes and their roles in various biological processes 18. The CAZy database has been instrumental in providing a stable nomenclature and classification system that aids in the functional prediction and annotation of these enzymes in genome projects .

Conclusion

Glycoside hydrolases are the primary enzymes responsible for the breakdown of carbohydrates, supported by polysaccharide lyases and carbohydrate esterases. The structural and functional diversity of these enzymes is vast, reflecting their crucial roles in nature. Resources like the CAZy database are invaluable for researchers studying these enzymes, providing detailed classifications and insights into their mechanisms and evolutionary relationships.

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Most relevant research papers on this topic

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

The CAZy database is a knowledge-based resource for glycogenomics, providing structural features, evolutionary relationships, and a framework for understanding mechanistic properties of enzymes involved in complex carbohydrates and glycoconjugates.

Highly Cited

2008·

7382citations

·B. Cantarel et al.

The carbohydrate-active enzymes database (CAZy) in 2013

CAZy, the carbohydrate-active enzymes database, has expanded to new families, developed subfamilies, and become a valuable tool for analyzing genomes and metagenomes.

Highly Cited

2013·

5271citations

·V. Lombard et al.

The continuing expansion of CAZymes and their families.

The number of CAZyme families continues to expand, revealing the massive diversity of glycans requiring diverse enzymes for their breakdown.

Highly Cited

2019·

119citations

·M. Garron et al.

A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana

Carbohydrate-active enzymes, particularly glycoside hydrolases and glycosyltransferases, play a crucial role in cell-wall formation and degradation in Arabidopsis thaliana, with at least 170 open reading frames dedicated to pectin degradation.

Highly Cited

2004·

132citations

·B. Henrissat et al.

Enzyme-catalyzed synthesis of carbohydrates.

New enzymes and improved methods for carbohydrate synthesis have been reported, with thermophilic enzymes showing potential advantages over mesophilic counterparts.

Highly Cited

2000·

76citations

·N Wymer et al.

Recent structural insights into the expanding world of carbohydrate-active enzymes.

Recent advances in understanding carbohydrate-active enzymes reveal diverse scaffolds and mechanisms, with glycoside hydrolases showing a wide variety of scaffolds and nucleotide-sugar-dependent glycosyltransferases grafted onto just two protein folds.

Highly Cited

2005·

305citations

·G. Davies et al.

Carbohydrate-active enzymes: sequences, shapes, contortions and cells.

Advances in glycosidase sequence discovery, classification, and 3D structures have provided new insights into enzyme catalysis, benefiting sustainable food and biofuel production, and advancing medicine and biotechnology.

2016·

44citations

·G. Davies et al.

Mechanistic analogies amongst carbohydrate modifying enzymes.

Understanding the chemical mechanisms of carbohydrate modifying enzymes can help design new therapeutic agents and aid in understanding the role of convergence in enzyme function evolution.

Highly Cited

2004·

93citations

·L. Lairson et al.

Reaction Mechanisms in Carbohydrate-Active Enzymes: Glycoside Hydrolases and Glycosyltransferases. Insights from ab Initio Quantum Mechanics/Molecular Mechanics Dynamic Simulations.

Recent advances in molecular dynamics simulations and density functional theory have significantly advanced our understanding of the catalytic mechanisms of glycoside hydrolases and glycosyltransferases, aiding in the development of efficient drug targets.

Highly Cited

2015·

192citations

·A. Ardèvol et al.

Structural diversity of carbohydrate esterases

Carbohydrate esterases (CEs) have diverse structures and enzymatic activities, but only a few have been studied biochemically and a few have their three-dimensional structures determined.

Highly Cited

2017·

112citations

·A. M. Nakamura et al.

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