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Difference between revisions of "Glycoside Hydrolase Family 121"

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|'''Mechanism'''
 
|'''Mechanism'''
|retaining/inverting
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|retaining
 
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|'''Active site residues'''
 
|'''Active site residues'''
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== Substrate specificities ==
 
== Substrate specificities ==
Content is to be added hereIn the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
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  0  0  1  17  97  鹿児島大学  1  1  113  14.0          Normal  0        10 pt  0  2    false  false  false    EN-US  JA  X-NONE                                                      $([\{£¥‘“〈《「『【〔$([{「£¥ !%),.:;?]}¢°’”‰′″℃、。々〉》」』】〕゛゜ゝゞ・ヽヾ!%),.:;?]}。」、・゙゚¢
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 +
This family of glycoside hydrolases was recently established for HypBA2 from
 +
 
 +
''Bifidobacterium longum'' JCM 1217   
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Content is to be added here.
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HypBA2 is a retaining enzyme.
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
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== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First stereochemistry determination: This was determined with HypBA2 enzyme using the 1H-NMR and 13C-NMR spectra of the transglycosylation product beta-Ara2-OMe.
;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 ==
 
== References ==

Revision as of 18:59, 26 April 2012

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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 GH121
Clan GH-x
Mechanism retaining
Active site residues known/not known
CAZy DB link
http://www.cazy.org/GH121.html


Substrate specificities

  0  0  1  17  97  鹿児島大学  1  1  113  14.0           Normal  0        10 pt  0  2    false  false  false    EN-US  JA  X-NONE                                                      $([\{£¥‘“〈《「『【〔$([{「£¥  !%),.:;?]}¢°’”‰′″℃、。々〉》」』】〕゛゜ゝゞ・ヽヾ!%),.:;?]}。」、・゙゚¢

This family of glycoside hydrolases was recently established for HypBA2 from

Bifidobacterium longum JCM 1217

Kinetics and Mechanism

HypBA2 is a retaining enzyme.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First stereochemistry determination
This was determined with HypBA2 enzyme using the 1H-NMR and 13C-NMR spectra of the transglycosylation product beta-Ara2-OMe.

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. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382

    [DaviesSinnott2008]