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Difference between revisions of "Glycoside Hydrolase Family 84"

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== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
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<cite>DJV2005</cite> <cite>DJV2009</cite>
  
  
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== References ==
 
== References ==
 
<biblio>
 
<biblio>
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#DJV2005 pmid=15795231
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#DJV2009 pmid=19715310
 
#GJD2006 pmid=16565725
 
#GJD2006 pmid=16565725
 
#DvA2006 pmid=16541109
 
#DvA2006 pmid=16541109

Revision as of 04:42, 29 June 2010

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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 GH84
Clan none
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/GH84.html


Substrate specificities

Content is to be added here.

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

[5] [6]


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.[7, 8]


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]
  5. Macauley MS, Whitworth GE, Debowski AW, Chin D, and Vocadlo DJ. (2005). O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors. J Biol Chem. 2005;280(27):25313-22. DOI:10.1074/jbc.M413819200 | PubMed ID:15795231 [DJV2005]
  6. Greig IR, Macauley MS, Williams IH, and Vocadlo DJ. (2009). Probing synergy between two catalytic strategies in the glycoside hydrolase O-GlcNAcase using multiple linear free energy relationships. J Am Chem Soc. 2009;131(37):13415-22. DOI:10.1021/ja904506u | PubMed ID:19715310 [DJV2009]
  7. Dennis RJ, Taylor EJ, Macauley MS, Stubbs KA, Turkenburg JP, Hart SJ, Black GN, Vocadlo DJ, and Davies GJ. (2006). Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity. Nat Struct Mol Biol. 2006;13(4):365-71. DOI:10.1038/nsmb1079 | PubMed ID:16565725 [GJD2006]
  8. Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, and van Aalten DM. (2006). Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 2006;25(7):1569-78. DOI:10.1038/sj.emboj.7601026 | PubMed ID:16541109 [DvA2006]

All Medline abstracts: PubMed