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 88

From CAZypedia
Revision as of 16:41, 3 April 2012 by Harry Brumer (talk | contribs)
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CAZypedia needs your help: This page is currently lacking a Responsible Curator and one or more Authors. If you are an expert on this family and would like to help us improve CAZypedia by getting involved with writing and maintaining this page, please contact the Primary Curator.

Undergraduate students, (post)graduate students, post-doctoral researchers, research associates, and professors are all welcomed to contribute!

  • If you are interested in contributing to CAZypedia, please see the 10th anniversary publication [1] and this page for an overview of the content and mission of our community-driven resource. Future authors of CAZypedia can include the CAZypedia article [1] and cite individual pages in their curricula vitae to reflect their contribution.
  • Until this CAZypedia page is completed, current information on the composition of this family is available via the corresponding page of the CAZy database [2]:
    http://www.cazy.org/GH88.html

References

  1. CAZypedia Consortium (2018). Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes. Glycobiology. 2018;28(1):3-8. DOI:10.1093/glycob/cwx089 | PubMed ID:29040563 [CAZypedia2018]
  2. Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, and Henrissat B. (2014). The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 2014;42(Database issue):D490-5. DOI:10.1093/nar/gkt1178 | PubMed ID:24270786 [CAZyDB2014]

All Medline abstracts: PubMed


Glycoside Hydrolase Family GH88
Clan GH-x
Mechanism retaining/inverting
Active site residues known/not known
CAZy DB link
http://www.cazy.org/GH88.html


Substrate specificities

Content is to be added here.

This is an example of how to make references to a journal article [3]. (See the References section below). Multiple references can go in the same place like this [3, 4]. You can even cite books using just the ISBN [5]. References that are not in PubMed can be typed in by hand [6].


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

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

    [Sinnott1990]

All Medline abstracts: PubMed