CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Glycoside Hydrolase Family 72

From CAZypedia
Jump to navigation Jump to search
Under construction icon-blue-48px.png

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 GH72
Clan none, (βα)8 fold
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/GH72.html


Substrate specificities

The GH72 family is formed exclusively by transglycosylases of the fungal kindgom whose activity was firstly characterized in Aspergillus fumigatus

The GH72 family is formed exclusively by transglycosylases of the fungal kindgom whose activity was firstly characterized in Aspergillus fumigatus [1] and yeasts [2, 3, 4]. These GPI-anchored plasma membrane enzymes elongate and remodel the β-1,3 glucan of the cell wall [4, 5, 6, 7, 8, 9]. This activity is due to their catalytic domain is located in the external part of the plasma membrane. Two sub-families have been described for GH72 family members depending on the presence or absence of a C-terminal cysteine rich domain (carbohydrate binding domain, CBM43) in addition to the catalytic domain [10]. This is an example of how to make references to a journal article [11]. (See the References section below). Multiple references can go in the same place like this [11, 12]. You can even cite books using just the ISBN [13]. References that are not in PubMed can be typed in by hand [14].


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 [11].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [14].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [12].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [13].

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