Beta-glucosidase

From Wikipedia, the free encyclopedia
β-glucosidase

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 / EGO

Beta-glucosidase (EC 3.2.1.21, gentiobiase, cellobiase, emulsin, elaterase, aryl-beta-glucosidase, beta-D-glucosidase, beta-glucoside glucohydrolase, arbutinase, amygdalinase, p-nitrophenyl beta-glucosidase, primeverosidase, amygdalase, linamarase, salicilinase, beta-1,6-glucosidase) is a glucosidase enzyme that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). It is 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]

Cellulose is largely composed of polymers of beta-bond linked glucose molecules, and beta-glucosidases are required by organisms (some fungi, bacteria, termites) 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)
Identifiers
Symbol GBA3
Alt. symbols CBGL1, KLRP
Entrez 57733
HUGO 19069
OMIM 606619
RefSeq NM_020973
UniProt Q9H227
Other data
Locus Chr. 4 p15.31

References

  1. ↑ PDB 3AHX; 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. doi:10.1016/j.jsb.2010.07.008. PMID 20682343. ; rendered via PyMOL.
  2. ↑ Cox, Michael; Lehninger, Albert L; Nelson, David R. (2000). Lehninger principles of biochemistry. New York: Worth Publishers. pp. 306–308. ISBN 1-57259-931-6. 

See also

External links

Hydrolase: sugar hydrolases (EC 3.2)
3.2.1: Glycoside hydrolases
Disaccharidase
Glucosidases
Other
3.2.2: Hydrolysing
N-Glycosyl compounds
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