The structure of beta-glucosidase A from bacterium Clostridium cellulovorans.
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
Beta-glucosidase is composed of two polypeptide chains. These two chains are chiral in nature meaning that the chains are asymmetric and not superimposable. Each chain is made up of 438 amino acids and constitute a subunit of the enzyme. Each of these subunits contain an active site. The active site serves as the location where an enzyme and substrate bind and an enzymatic reaction can occur. The active site has three potential components: the pocket, the cleft, and the tunnel. The pocket structure is beneficial for recognition of monosaccharide like glucose. The cleft is allows for binding of sugars to form polysaccharides. The tunnel allows for the enzyme to attach to polysaccharide and then release product while still attached to the sugar.
The function of the enzyme is preform hydrolysis of various glycosides and oligosaccharides. The most significant oligosaccharide beta-glucosidase reacts with is cellulose. Cellulose is a polymer composed of beta-1,4-linked glucosyl residues. Beta-glucosidases, Cellulases (endoglucanases), cellobiosidases (exoglucanases) are required by a number of organisms to consume it. These enzymes are powerful tools for degradation of plant cell walls by pathogens and other organisms consuming plant biomass. Beta glucosidases are essential for many organisms to digest a variety of nutrients. This enzyme completes double-displacement reaction, meaning that the enzyme is changed to an intermediate form when the first substrate enters the active site, it then releases the product before another substrate binds, and reverts to its original form by the end of the reaction. In the case of beta-glucosidase, two carboxylate residues of glucosides, cellobiose, cellotriose, cellotetraose are involved at the active site. The purpose of the reaction is to remove the residues from disaccharide cellobiose to produce glucose during the hydrolysis of biomass. Depending on the what the enzyme is reacting with the end product will be one or two glucose molecules.
Humans are unable to digest cellulose of plants cells. This is because the enzyme is not present in the human stomach, as the optimal pH is 5.6, while the pH of a human's stomach is acidic (between 1.5 and 3.5). However, humans do require beta-glucosidase, Lysosomal β-glucosidase, as it plays an important role in the degradation of glycosphingolipids. The enzyme will break down glucosylceramide into ceramide and glucose. If an accumulation occurs this will lead to Gaucher disease. The buildup of fatty substances can lead to weakening bones, liver damage, and enlarging and imparing the function the spleen.
Bonnethead sharks are found in tropical and subtropical water living in estuaries with muddy or sandy bottoms, rich with seagrass. They were once thought of as being solely carnivores. It was known that bonnethead did consume seagrass, but it was viewed as incidental and dismissed as not helping the benefitting the shark. However, recent studies of the shark's hindgut has found that it has a high activity level of beta glucosidase. During the digestive process of the bonnethead shark, the acidic stomach weakens the cell walls of the seagrass and allows for beta-glucosidase to enter the cell and digest the cellulose. The activity level is on par with the monkeyface eel. The monkeyface eel is an herbivore, meaning that the bonnethead is able to preform the same digestive activity has an organism that is an herbivore. Therefore, the bonnethead shark is now classified as an omnivore.
Christmas Island Red Crab
The Christmas Island red crab is a species of crab located solely in the Christmas Island of the Indian Ocean. Land crabs such as these possess multiple varieties of Beta-glucosidase as they are terrestrial herbivores. In the case of the Christmas Island red crab beta glucosidase not only produces glucose, but also removes cellobiose. This is important as cellobiose is an inhibitor for a number of enzymes including endo-β-1,4-glucanase and cellobiohydrolase. Beta-glucosidase is also capable completeling [sic?] hydrolysis on small oligomers that are produced by other enzymes without the assistance of an intermediate enzyme. This in turn makes beta glucosidase a very efficient enzyme in not only the digestive tract of the Christmas Island red crab, but other crustaceans as well.
Synonyms, derivatives, and related enzymes include gentiobiase, cellobiase, emulsin, elaterase, aryl-beta-glucosidase, beta-D-glucosidase, beta-glucoside glucohydrolase, arbutinase, amygdalinase, p-nitrophenyl beta-glucosidase, primeverosidase, amygdalase, linamarase, salicilinase, and beta-1,6-glucosidase.
|glucosidase, beta, acid 3 (cytosolic)|
|Alt. symbols||CBGL1, KLRP|
|Locus||Chr. 4 p15.31|
- Amygdalin beta-glucosidase
- Cellulase, a suite of enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis (i.e. the hydrolysis of cellulose)
- Glucosylceramidase, a related enzyme
- Prunasin beta-glucosidase
- Vicianin beta-glucosidase
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- GO-database listing 'GO:0016162 cellulose 1,4-beta-cellobiosidase activity'
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