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Difference between revisions of "Glycoside Hydrolase Family 44"

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[http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
 
[http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
  
Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282:35703–35711.  
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#Kitago2007 Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282:35703–35711.  
 
</biblio>
 
</biblio>
  
 
[[Category:Glycoside Hydrolase Families|GH044]]
 
[[Category:Glycoside Hydrolase Families|GH044]]

Revision as of 11:13, 13 August 2010

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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 GH44
Clan None specified
Mechanism Retaining
Active site residues


CAZy DB link
https://www.cazy.org/GH44.html


Substrate specificities

Content is to be added here.

This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].


Kinetics and Mechanism

Content is to be added here.


Catalytic Residues

Clostridium thermocellum: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Clostridium acetobutylicum: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352


Three-dimensional structures

Content is to be added here.


Family Firsts

First stereochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [1].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [4].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [2].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [3].

References

  1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n | PubMed ID:17323919 [Comfort2007]
  2. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 | PubMed ID:9312086 [He1999]
  3. [StickWilliams]
  4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202.

    DOI: 10.1021/cr00105a006

    [Sinnott1990]
  5. Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282:35703–35711.

    [Kitago2007]

All Medline abstracts: PubMed