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Difference between revisions of "Glycoside Hydrolase Family 136"

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(Changed RC and author following email exchanges with Shinya and Ana)
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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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== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
+
The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==

Revision as of 19:39, 10 August 2020

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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 GH136
Clan GH-x
Mechanism retaining
Active site residues known
CAZy DB link
https://www.cazy.org/GH136.html


Substrate specificities

Content is to be added here.

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: [1, 2].

Kinetics and Mechanism

Content is to be added here.

Catalytic Residues

The nucleophile is Asp418. The catalytic acid/base is Asp411 via water molecule.

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. 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]
  2. 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]