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Difference between revisions of "Glycoside Hydrolase Family 29"

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== Substrate specificities ==
 
== Substrate specificities ==
The glycoside hydrolases of this family are exo-acting α-fucosidases from archaeal, bacterial and eukaryotic origin.
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The glycoside hydrolases of this family are exo-acting α-fucosidases from archaeal, bacterial and eukaryotic origin.               Normal.dotm  0  0  1  5  33  AFMB  1  1  40  12.0              0  false      21      18 pt  18 pt  0  0      false  false  false
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No other activities have been observed.                Normal.dotm  0  0  1  17  101  AFMB  1  1  124  12.0              0  false      21      18 pt  18 pt  0  0      false  false  false                                    The human enzyme is of medical interest because its deficiency leads to fucosidosis, a autosomal recessive lysosomal storage disease.
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This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below).  Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>.  You can even cite books using just the ISBN <cite>3</cite>.  References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>.   
 
This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below).  Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>.  You can even cite books using just the ISBN <cite>3</cite>.  References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>.   

Revision as of 08:52, 28 October 2009

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Glycoside Hydrolase Family GHnn
Clan none
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GHnn.html


Substrate specificities

The glycoside hydrolases of this family are exo-acting α-fucosidases from archaeal, bacterial and eukaryotic origin. Normal.dotm 0 0 1 5 33 AFMB 1 1 40 12.0 0 false 21 18 pt 18 pt 0 0 false false false

No other activities have been observed. Normal.dotm 0 0 1 17 101 AFMB 1 1 124 12.0 0 false 21 18 pt 18 pt 0 0 false false false The human enzyme is of medical interest because its deficiency leads to fucosidosis, a autosomal recessive lysosomal storage disease.


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

Content is to be added here.


Three-dimensional structures

Content is to be added here.


Family Firsts

First sterochemistry 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. Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science. [3]
  4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [MikesClassic]

All Medline abstracts: PubMed

[[Category:Glycoside Hydrolase Families|GHnnn]]