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Difference between revisions of "Glycoside Hydrolase Family 35"

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Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.
 
Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.
 
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>. 
 
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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<biblio>
 
<biblio>
 
#Tanthanuch2008 pmid=18664295
 
#Tanthanuch2008 pmid=18664295
 +
#Kawarabayasi1998 pmid=96794
 +
#Fukui2005 pmid=15710748
  
 +
 
#Comfort2007 pmid=17323919
 
#Comfort2007 pmid=17323919
 
#He1999 pmid=9312086
 
#He1999 pmid=9312086

Revision as of 03:12, 4 October 2010

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Glycoside Hydrolase Family GH35
Clan GH-A
Mechanism retaining (inferred)
Active site residues known
CAZy DB link
https://www.cazy.org/GH35.html


Substrate specificities

The major activity of enzymes of this GH family is β-galactosidase (EC 3.2.1.23). Enzymes were isolated from microorganisms such as fungi, bacteria and yeasts; plants, animals cells, and from recombinant sources. The β-galactosidase (EC 3.2.1.23) catalyses the hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides as, for example, lactose (1,4-O-β-D-galactopyranosyl-D-glucose) and structurally related compounds. GH35 includes multiple genes in various plant species [1], suggesting ubiquity of GH35 gene multiplicity in plants. The enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production of galactosylated products.

Besides β-galactosidases, GHF35 contains two exo-β-glucosaminidases (EC 3.2.1.165) [2,3]. This enzyme hydrolyze chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.

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

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. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006

    [Sinnott1990]
  3. 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]
  4. [StickWilliams]
  5. Tanthanuch W, Chantarangsee M, Maneesan J, and Ketudat-Cairns J. (2008). Genomic and expression analysis of glycosyl hydrolase family 35 genes from rice (Oryza sativa L.). BMC Plant Biol. 2008;8:84. DOI:10.1186/1471-2229-8-84 | PubMed ID:18664295 [Tanthanuch2008]
  6. Davis E (1978). Vaccine damaged children. Australas Nurses J. 1978;7(8):3-6. | Google Books | Open Library PubMed ID:96794 [Kawarabayasi1998]
  7. Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S, and Imanaka T. (2005). Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 2005;15(3):352-63. DOI:10.1101/gr.3003105 | PubMed ID:15710748 [Fukui2005]

All Medline abstracts: PubMed