Glycoside hydrolase family 2
Encyclopedia
In molecular biology, Glycoside hydrolase family 2 is a family
Protein family
A protein family is a group of evolutionarily-related proteins, and is often nearly synonymous with gene family. The term protein family should not be confused with family as it is used in taxonomy....

 of glycoside hydrolases
Glycoside hydrolase
Glycoside hydrolases catalyze the hydrolysis of the glycosidic linkage to release smaller sugars...

.

Glycoside hydrolases  are a widespread group of enzymes that hydrolyse the glycosidic bond
Glycosidic bond
In chemistry, a glycosidic bond is a type of covalent bond that joins a carbohydrate molecule to another group, which may or may not be another carbohydrate....

 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(http://www.cazy.org/GH1.html) web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.

Glycoside hydrolase family 2 comprises enzymes with several known activities: beta-galactosidase
Beta-galactosidase
β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins...

 (EC 3.2.1.23); beta-mannosidase (EC 3.2.1.25); beta-glucuronidase (EC 3.2.1.31). These enzymes contain a conserved glutamic acid residue which has been shown, in Escherichia coli
Escherichia coli
Escherichia coli is a Gram-negative, rod-shaped bacterium that is commonly found in the lower intestine of warm-blooded organisms . Most E. coli strains are harmless, but some serotypes can cause serious food poisoning in humans, and are occasionally responsible for product recalls...

lacZ , to be the general acid/base catalyst in the active site of the enzyme.

The catalytic domain of Beta-galactosidases have a TIM barrel
TIM barrel
The TIM barrel is a conserved protein fold consisting of eight α-helices and eight parallel β-strands that alternate along the peptide backbone. The structure is named after triosephosphate isomerase, a conserved glycolytic enzyme. TIM barrels are quite common among the conserved protein folds...

 core surrounded several other largely beta domains. The sugar binding domain of these proteins has a jelly-roll fold. These enzymes also include an immunoglobulin-like beta-sandwich domain.

External references

GH2 in CAZypedia
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