Beta-glucosidase

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β-glucosidase
Beta glucosidase 3AHX.png
The structure of beta-glucosidase A from bacterium Clostridium cellulovorans.[1]
Identifiers
EC number3.2.1.21
CAS number9001-22-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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
SymbolGBA3
Alt. symbolsCBGL1, KLRP
Entrez57733
HUGO19069
OMIM606619
RefSeqNM_020973
UniProtQ9H227
Other data
EC number3.2.1.21
LocusChr. 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]