Biology:Glucosidases

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Short description: Enzymes which hydrolyse glycosides

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Beta-amylase, a type of glucosidase

Glucosidases are the glycoside hydrolase enzymes categorized under the EC number 3.2.1.[1]

Function

Alpha-glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen into their monomers.[2]

They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or beta-linked polymers of glucose. This enzyme convert complex sugars into simpler ones.

Members

Different sources include different members in this class. Members marked with a "#" are considered by MeSH to be glucosidases.

Name EC Description
α-Amylase EC 3.2.1.1 is a digestive enzyme in mammals
β-Amylase EC 3.2.1.2 is a plant enzyme to break down starch
γ-Amylase EC 3.2.1.3 is a digestive enzyme
Cellulase # EC 3.2.1.4 breaks down cellulose from plant material
Sucrase-isomaltase EC 3.2.1.10 -
Mannosyl-oligosaccharide glucosidase # EC 3.2.1.106 catalyzes the first trimming step of the N-glycosylation pathway; is associated with Congenital Disorder of Glycosylation type IIb
Acid α-glucosidase # EC 3.2.1.20 is associated with Glycogen storage disease type II
Beta-glucosidase # EC 3.2.1.21 is associated with Gaucher's disease
Lactase EC 3.2.1.23 one member of the β-galactosidase family, breaks down milk sugars, and its absence in adulthood causes lactose intolerance
Debranching enzyme # EC 3.2.1.33 in mammals, yeast and some bacteria, combines transferase and glucosidase activity in glycogen breakdown
Pullulanase EC 3.2.1.41 has been used as a detergent

Clinical significance

Alpha-glucosidases are targeted by alpha-glucosidase inhibitors such as acarbose and miglitol to control diabetes mellitus type 2.

See also

  • DNA glycosylases
  • Mucopolysaccharidoses

References

  1. "ENZYME class: 3.2.1". SIB Swiss Institute of Bioinformatics. June 2021. https://enzyme.expasy.org/EC/3.2.1.-. 
  2. Krasikov, V. V.; Karelov, D. V.; Firsov, L. M. (March 2001). "α-Glucosidases". Biochemistry (Moscow) 66 (3): 267–281. doi:10.1023/A:1010243611814. PMID 11333149. http://link.springer.com/10.1023/A:1010243611814. 

External links