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EntityQ3266947· pop 12· linked from 369 articles

beta-glucosidase

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Also known as beta-D-glucoside glucohydrolase, beta-D-glucosidase, beta-1,6-glucosidase, p-nitrophenyl beta-glucosidase, arbutinase, beta-glucoside glucohydrolase, aryl-beta-glucosidase

β-Glucosidase (; systematic name β-D-glucoside glucohydrolase) is an enzyme that catalyses the following reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose

Key facts

Enzyme.Name
β-Glucosidase
Enzyme.EC_number
3.2.1.21
Enzyme.CAS_number
9001-22-3
Enzyme.GO_code
0008422
Enzyme.image
Beta_glucosidase_3AHX.png
Enzyme.caption
The structure of β-glucosidase A from bacterium Clostridium cellulovorans.
Protein.Name
glucosidase, beta, acid 3 (cytosolic)
Protein.HGNCid
19069
Protein.Symbol
GBA3
Protein.AltSymbols
CBGL1, KLRP
Protein.EntrezGene
57733
Protein.OMIM
606619
Protein.RefSeq
NM_020973
Protein.UniProt
Q9H227
Protein.ECnumber
3.2.1.21
Protein.Chromosome
4
Protein.Arm
p
Protein.Band
15.31

via Wikipedia infobox

~6 min read

Encyclopedic overview

9 sections
Contents
  • Structure
  • Function
  • Humans
  • Bonnethead Shark
  • Christmas Island Red Crab
  • Synonyms
  • See also
  • References
  • External links

β-Glucosidase (; systematic name β-D-glucoside glucohydrolase) is an enzyme that catalyses the following reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose

== Structure == β-Glucosidase is composed of two polypeptide chains. Each chain is made up of 438 amino acids and constitute a subunit of the enzyme. Each of these subunits contains an active site. 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 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.

Excerpted from Wikipedia’s “beta-glucosidase” article, available under the CC BY-SA 4.0 licence.