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Difference between revisions of "Glycoside Hydrolase Family 107"

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|'''Clan'''     
 
|'''Clan'''     
|GH-x
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|GH-R
 
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|'''Mechanism'''
 
|'''Mechanism'''
|retaining/inverting
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|retaining
 
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|'''Active site residues'''
 
|'''Active site residues'''
|known/not known
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|known
 
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|{{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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The [[glycoside hydrolases]] of this family are [[endo]]-acting α-fucosidases active on sulfated fucans (or fucoidans) from brown algae.
  
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...)''
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All described GH107 family members are endo-1,4-fucanase of bacterial origin.
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
  
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With enzymes from the CAZY family [[GH29]] they form the clan GH-R.
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
 
Content is to be added here.
 
Content is to be added here.
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
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The catalytic nucleophile is an aspartate, while the catalytic acid-base is a histidine. The later is unusual in GHs, and a divergence from [[GH29]], but is likely necessary to avoid electronic repulsion with the substrate sulfate groups.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==

Revision as of 09:41, 12 December 2019

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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 GH107
Clan GH-R
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/GH107.html


Substrate specificities

The glycoside hydrolases of this family are endo-acting α-fucosidases active on sulfated fucans (or fucoidans) from brown algae.

All described GH107 family members are endo-1,4-fucanase of bacterial origin.

With enzymes from the CAZY family GH29 they form the clan GH-R.

Kinetics and Mechanism

Content is to be added here.

Catalytic Residues

The catalytic nucleophile is an aspartate, while the catalytic acid-base is a histidine. The later is unusual in GHs, and a divergence from GH29, but is likely necessary to avoid electronic repulsion with the substrate sulfate groups.

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. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 | PubMed ID:18838391 [Cantarel2009]
  2. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.

    [DaviesSinnott2008]