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Difference between revisions of "Glycoside Hydrolase Family 164"

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== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First sterochemistry determination: ''Bacteroides salyersiae'' β-mannosidase by NMR <cite>Armstrong2020</cite>
;First catalytic nucleophile identification: Content is to be added here.
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;First [[catalytic nucleophile]] identification: ''Bacteroides salyersiae'' β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants <cite>Armstrong2020</cite>
;First general acid/base residue identification: Content is to be added here.
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;First [[general acid/base]] residue identification: ''Bacteroides salyersiae'' β-mannosidase by kinetic analysis of mutants <cite>Armstrong2020</cite>
;First 3-D structure: Content is to be added here.
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;First 3-D structure of a GH1 enzyme: ''Bacteroides salyersiae'' β-mannosidase <cite>Armstrong2020</cite>
 
 
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>

Revision as of 08:18, 2 April 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 GH164
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
https://www.cazy.org/GH164.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

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First sterochemistry determination
Bacteroides salyersiae β-mannosidase by NMR [3]
First catalytic nucleophile identification
Bacteroides salyersiae β-mannosidase by 2-fluoromannose labeling and kinetic analysis of mutants [3]
First general acid/base residue identification
Bacteroides salyersiae β-mannosidase by kinetic analysis of mutants [3]
First 3-D structure of a GH1 enzyme
Bacteroides salyersiae β-mannosidase [3]

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]