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Difference between revisions of "Glycoside Hydrolase Family 75"

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== Substrate specificities ==
 
== Substrate specificities ==
Glycoside hydrolases of family 75 are primarily of endo-beta-1,4-chitosanases <cite>Shimosaka1993 Cheng2000</cite>.
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Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from fimanetous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</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>StickWilliams</cite>.  References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. 
 
  
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== Kinetics and Mechanism ==
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Family GH46 enzymes utilize an inverting mechanism as shown by NMR <cite>Chend2006</cite>.
  
== Kinetics and Mechanism ==
 
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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>StickWilliams</cite>.  References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>.
  
 
== Family Firsts ==
 
== Family Firsts ==

Revision as of 10:58, 3 June 2011

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Glycoside Hydrolase Family GH75
Clan GH-x
Mechanism inverting
Active site residues known/not known
CAZy DB link
https://www.cazy.org/GH75.html


Substrate specificities

Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from fimanetous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity [1, 2].

Kinetics and Mechanism

Family GH46 enzymes utilize an inverting mechanism as shown by NMR [3].


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.

This is an example of how to make references to a journal article [4]. (See the References section below). Multiple references can go in the same place like this [4, 5]. You can even cite books using just the ISBN [6]. References that are not in PubMed can be typed in by hand [7].

Family Firsts

First stereochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [4].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [7].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [6].

References

  1. Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, Fusarium solani f.sp. phaseoli - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.

    [Shimosaka1993]
  2. Cheng CY and Li YK. (2000). An Aspergillus chitosanase with potential for large-scale preparation of chitosan oligosaccharides. Biotechnol Appl Biochem. 2000;32(3):197-203. DOI:10.1042/ba20000063 | PubMed ID:11115392 [Cheng2000]
  3. 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]
  4. 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]
  5. [StickWilliams]
  6. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [Sinnott1990]

All Medline abstracts: PubMed