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Difference between revisions of "Glycoside Hydrolase Family 120"

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|-
 
|-
 
|'''Clan'''     
 
|'''Clan'''     
|GH-x
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|none
 
|-
 
|-
 
|'''Mechanism'''
 
|'''Mechanism'''
|retaining/inverting
+
|retaining
 
|-
 
|-
 
|'''Active site residues'''
 
|'''Active site residues'''
|known/not known
+
|known
 
|-
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
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== Substrate specificities ==
 
== Substrate specificities ==
Content is to be added here.
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[[Glycoside hydrolases]] of family GH120 are &beta;-xylosidases. XylC from ''Thermoanaerobacterium saccharolyticum'' hydrolyzed xylobiose and xylotriose, and aryl &beta;-xylosides <cite>Shao2011</cite>. No activity was detected on oat spelt or birch wood xylans. Both ''T. saccharolyticum'' XylC and XylB from ''Bifidobacterium adolescentis'' can hydrolyze assorted aryl &beta;-xylosides <cite>Shao2011 Cecchini2015</cite>.
 
 
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
 
  
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
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#Huang2012 pmid=22992047
 
#Huang2012 pmid=22992047
 
#Shao2011 pmid=21131522
 
#Shao2011 pmid=21131522
 +
#Cecchini2015 pmid=26297820
 
</biblio>
 
</biblio>
  
 
[[Category:Glycoside Hydrolase Families|GH120]]
 
[[Category:Glycoside Hydrolase Families|GH120]]

Revision as of 20:32, 24 November 2016

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH120
Clan none
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/GH120.html


Substrate specificities

Glycoside hydrolases of family GH120 are β-xylosidases. XylC from Thermoanaerobacterium saccharolyticum hydrolyzed xylobiose and xylotriose, and aryl β-xylosides [1]. No activity was detected on oat spelt or birch wood xylans. Both T. saccharolyticum XylC and XylB from Bifidobacterium adolescentis can hydrolyze assorted aryl β-xylosides [1, 2].

In the meantime, please see these references for an essential introduction to the CAZy classification system: [3, 4].

Kinetics and Mechanism

Content is to be added here.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First stereochemistry determination
Content is to be added here.
First catalytic nucleophile identification
Content is to be added here.
First general acid/base residue identification
Content is to be added here.
First 3-D structure
Content is to be added here.

References

  1. Shao W, Xue Y, Wu A, Kataeva I, Pei J, Wu H, and Wiegel J. (2011). Characterization of a novel beta-xylosidase, XylC, from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Appl Environ Microbiol. 2011;77(3):719-26. DOI:10.1128/AEM.01511-10 | PubMed ID:21131522 [Shao2011]
  2. Cecchini DA, Fauré R, Laville E, and Potocki-Veronese G. (2015). Biochemical identification of the catalytic residues of a glycoside hydrolase family 120 β-xylosidase, involved in xylooligosaccharide metabolisation by gut bacteria. FEBS Lett. 2015;589(20 Pt B):3098-106. DOI:10.1016/j.febslet.2015.08.012 | PubMed ID:26297820 [Cecchini2015]
  3. Huang CH, Sun Y, Ko TP, Chen CC, Zheng Y, Chan HC, Pang X, Wiegel J, Shao W, and Guo RT. (2012). The substrate/product-binding modes of a novel GH120 β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485. Biochem J. 2012;448(3):401-7. DOI:10.1042/BJ20121359 | PubMed ID:22992047 [Huang2012]

All Medline abstracts: PubMed