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β-glucosidase
Beta glucosidase 3AHX.png
The structure of beta-glucosidase A from bacterium Clostridium cellulovorans.[1]
Identifiers
EC number 3.2.1.21
CAS number 9001-22-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

Beta-glucosidase catalyzes the hydrolysis of the glycosidic bonds to terminal non-reducing residues in beta-D-glucosides and oligosaccharides, with release of glucose.[2]

Synonyms, derivatives, and related enzymes include gentiobiase, cellobiase, emulsin,[3] 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.

Cellulose is a polymer composed of beta-1,4-linked glucosyl residues. Cellulases (endoglucanases), cellobiosidases (exoglucanases), and beta-glucosidases are required by organisms (some fungi, bacteria) that can consume it. These enzymes are powerful tools for degradation of plant cell walls by pathogens and other organisms consuming plant biomass.


glucosidase, beta, acid 3 (cytosolic)
Identifiers
Symbol GBA3
Alt. symbols CBGL1, KLRP
Entrez 57733
HUGO 19069
OMIM 606619
RefSeq NM_020973
UniProt Q9H227
Other data
EC number 3.2.1.21
Locus Chr. 4 p15.31

See also[edit]

References[edit]

  1. ^ PDB: 3AHX​; Jeng WY, Wang NC, Lin MH, Lin CT, Liaw YC, Chang WJ, Liu CI, Liang PH, Wang AH (January 2011). "Structural and functional analysis of three β-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis". Journal of Structural Biology. 173 (1): 46–56. doi:10.1016/j.jsb.2010.07.008. PMID 20682343. ; rendered via PyMOL.
  2. ^ Cox M, Lehninger AL, Nelson DR (2000). Lehninger principles of biochemistry. New York: Worth Publishers. pp. 306–308. ISBN 1-57259-931-6. 
  3. ^ Mann FG, Saunders BC (1975). Practical Organic Chemistry (4th ed.). London: Longman. pp. 509–517. ISBN 9788125013808. Retrieved 1 February 2016. 

External links[edit]

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