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Title: Beta-glucosidase  
Author: World Heritage Encyclopedia
Language: English
Subject: Cellulase, N-Octyl beta-D-thioglucopyranoside, Piceid, HEXB, Acid alpha-glucosidase
Collection: Ec 3.2.1
Publisher: World Heritage Encyclopedia


The structure of beta-glucosidase A from bacterium Clostridium cellulovorans.[1]
EC number
CAS number 9001-22-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

Beta-glucosidase is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is one of the cellulases, enzymes involved in the decomposition of cellulose and related polysaccharides; more specifically, an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose.[2]

Synonyms, derivatives, and related enzymes include gentiobiase, cellobiase, emulsin, elaterase, aryl-beta-glucosidase, beta-D-glucosidase, beta-glucoside glucohydrolase, arbutinase, amygdalinase, p-nitrophenyl beta-glucosidase, primeverosidase, amygdalase, linamarase, salicilinase, and beta-1,6-glucosidase.

fungi, bacteria) that can consume it. These enzymes are a powerful tool for degradation of plant cell walls for pathogens.

Lysozyme, an enzyme secreted in tears to prevent bacterial infection of the eye, is also a beta-glucosidase that cleaves β1→4 bonds between N-acetylglucosamine and N-acetylmuramic acid sugars within the peptidoglycan cell walls of gram-negative bacteria.

glucosidase, beta, acid 3 (cytosolic)
Symbol GBA3
Alt. symbols CBGL1, KLRP
Entrez 57733
HUGO 19069
OMIM 606619
RefSeq NM_020973
UniProt Q9H227
Other data
EC number
Locus Chr. 4 p15.31


  1. ^ ​; Jeng, W.-Y., Wang, N.-C., Lin, M.-H., Lin, C.-T., Liaw, Y.-C., Chang, W.-J., Liu, C.-I., Liang, P.-H., Wang, A.H.-J. (August 2010). "Structural and functional analysis of three beta-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis.". J.Struc.Biol. 173 (1): 46–56.  ; rendered via PyMOL.
  2. ^ Cox, Michael; Lehninger, Albert L; Nelson, David R. (2000). Lehninger principles of biochemistry. New York: Worth Publishers. pp. 306–308.  

See also

External links

  • beta-Glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
  • GO-database listing 'GO:0016162 cellulose 1,4-beta-cellobiosidase activity'
  • Risk Assessment Summary, CEPA 1999. P59GTrichoderma reesei
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