Glucosidase

Glucosidases

Glucosidases

Enzymes which hydrolyse glycosides

Not to be confused with Glycosidase.

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

Beta-amylase, a type of glucosidase

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.

NameECDescription
α-AmylaseEC 3.2.1.1 is a digestive enzyme in mammals
β-AmylaseEC 3.2.1.2 is a plant enzyme to break down starch
γ-AmylaseEC 3.2.1.3 is a digestive enzyme
Cellulase #EC 3.2.1.4 breaks down cellulose from plant material
Sucrase-isomaltaseEC 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
LactaseEC 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 3.2.1.33in mammals, yeast and some bacteria, combines transferase and glucosidase activity in glycogen breakdown
PullulanaseEC 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

References

  1. [1]
    "ENZYME class: 3.2.1". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. June 2021. Retrieved 2021-09-13.
  2. [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.
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