Beta-glucosidase
| 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 / 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
- Amygdalin beta-glucosidase
- Cellulase, a suite of enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis (i.e. the hydrolysis of cellulose)
- Glucosylceramidase, a related enzyme
- Prunasin beta-glucosidase
- Vicianin beta-glucosidase
References
- ↑ 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.
- ↑ Cox M, Lehninger AL, Nelson DR (2000). Lehninger principles of biochemistry. New York: Worth Publishers. pp. 306–308. ISBN 1-57259-931-6.
- ↑ Mann FG, Saunders BC (1975). Practical Organic Chemistry (4th ed.). London: Longman. pp. 509–517. ISBN 9788125013808. Retrieved 1 February 2016.
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. Trichoderma reesei P59G