Beta-glucosidase: Difference between revisions

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| image = Beta_glucosidase_3AHX.png
| image = Beta_glucosidase_3AHX.png
| width =  
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| caption = The structure of beta-glucosidase A from bacterium ''Clostridium cellulovorans''.<ref name="pmid20682343 ">{{PDB|3AHX}}; {{cite journal | author = Jeng, W.-Y. | author2 = Wang, N.-C. | author3 = Lin, M.-H. | author4 = Lin, C.T. | author5 = Liaw, Y.C. | author6 = Chang, W.J. | author7 = Liu, C.I. | author8 = Liang, P.H. | author9 = Wang A.H.J.| title = Structural and functional analysis of three beta-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis. | journal = J.Struc.Biol. |date=August 2010 | pmid = 20682343 | doi = 10.1016/j.jsb.2010.07.008 | url = | issn = | volume = 173 | pages = 46–56 | issue = 1 }}; rendered via [http://pymol.sourceforge.net PyMOL].</ref>
| caption = The structure of beta-glucosidase A from bacterium ''Clostridium cellulovorans''.<ref name="pmid20682343 ">{{PDB|3AHX}}; {{cite journal | vauthors = Jeng WY, Wang NC, Lin MH, Lin CT, Liaw YC, Chang WJ, Liu CI, Liang PH, Wang AH | title = Structural and functional analysis of three β-glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis | journal = Journal of Structural Biology | volume = 173 | issue = 1 | pages = 46–56 | date = January 2011 | pmid = 20682343 | doi = 10.1016/j.jsb.2010.07.008 }}; rendered via [http://pymol.sourceforge.net PyMOL].</ref>
}}
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'''Beta-glucosidase''' catalyzes the hydrolysis of the glycosidic bonds to terminal non-reducing residues in beta-D-glucosides and oligosaccharides, with release of glucose.<ref name="isbn1-57259-931-6">{{cite book |author1=Cox, Michael |author2=Lehninger, Albert L |author3=Nelson, David R. | title = Lehninger principles of biochemistry | edition = | language = | publisher = Worth Publishers | location = New York | year = 2000 | origyear = | pages = 306–308 | quote = | isbn = 1-57259-931-6 | oclc = | doi = | url = | accessdate = }}</ref>
'''Beta-glucosidase''' catalyzes the hydrolysis of the glycosidic bonds to terminal non-reducing residues in beta-D-glucosides and oligosaccharides, with release of glucose.<ref name="isbn1-57259-931-6">{{cite book | last1 = Cox | first1 = Michael | last2 = Lehninger | first2 = Albert L | last3 = Nelson | first3 = David R. | name-list-format = vanc | title = Lehninger principles of biochemistry | edition = | publisher = Worth Publishers | location = New York | year = 2000 | origyear = | pages = 306–308 | quote = | isbn = 1-57259-931-6 | oclc = | doi = | url = | accessdate = }}</ref>


Synonyms, derivatives, and related enzymes include '''gentiobiase''', '''[[cellobiase]]''', '''emulsin''',<ref>{{cite book|last1=George Mann|first1=Frederick|last2=Charles Saunders|first2=Bernard|title=Practical Organic Chemistry|date=1975|publisher=Longman|location=London|isbn=9788125013808|pages=509–517|edition=4th|url=http://www.sciencemadness.org/talk/files.php?pid=385854&aid=36353|accessdate=1 February 2016}}</ref> '''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'''.
Synonyms, derivatives, and related enzymes include '''gentiobiase''', '''[[cellobiase]]''', '''emulsin''',<ref>{{cite book|last1=Mann|first1=Frederick George |last2=Saunders|first2=Bernard Charles | name-list-format = vanc |title=Practical Organic Chemistry|date=1975|publisher=Longman|location=London|isbn=9788125013808|pages=509–517|edition=4th|url=http://www.sciencemadness.org/talk/files.php?pid=385854&aid=36353|accessdate=1 February 2016}}</ref> '''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. [[Cellulase]]s ([[endoglucanase]]s), [[cellobiosidase]]s ([[exoglucanase]]s), 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.
[[Cellulose]] is a polymer composed of beta-1,4-linked glucosyl residues. [[Cellulase]]s ([[endoglucanase]]s), [[cellobiosidase]]s ([[exoglucanase]]s), 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.
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* [[Vicianin beta-glucosidase]]
* [[Vicianin beta-glucosidase]]


==References==
== References ==
{{Reflist}}
{{Reflist}}


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[[Category:EC 3.2.1]]
[[Category:EC 3.2.1]]
[[Category:Enzymes of known structure]]
[[Category:Enzymes of known structure]]


{{3.2-enzyme-stub}}
{{3.2-enzyme-stub}}

Latest revision as of 11:52, 10 January 2019

β-glucosidase
File: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

References

  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

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