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Glycoside Hydrolase Family 120

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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

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First stereochemistry determination
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First catalytic nucleophile identification
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First general acid/base residue identification
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First 3-D structure
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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