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Glycoside hydrolase family 78
| Field | Value |
|---|---|
| Symbol | Bac_rhamnosid |
| Name | Bacterial alpha-L-rhamnosidase |
| Pfam | PF05592 |
| Pfam_clan | CL0059 |
| InterPro | IPR008902 |
| CAZy | GH78 |
In molecular biology, glycoside hydrolase family 78 is a family of glycoside hydrolases.
Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of 100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.
Glycoside hydrolase family 78 CAZY GH_78 includes enzymes with α-L-rhamnosidase activity. This family includes bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
References
References
- (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America.
- (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure.
- (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal.
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- (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research.
- "Glycoside Hydrolase Family 78".
- (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology.
- (January 2000). "The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase". Mol. Microbiol..
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