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Difference between revisions of "Glycoside Hydrolase Family 6"

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== Substrate specificities ==
 
== Substrate specificities ==
Endoglucanases (EC 3.2.1.4) and cellobiohydrolases (EC 3.2.1.91)only.  Both classes of enzyme active on cellulose / beta 1,4 glucans.  
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Endoglucanases (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolases (EC [{{EClink}}3.2.1.91 3.2.1.91])only.  Both classes of enzyme active on cellulose / beta 1,4 glucans.  
  
  

Revision as of 06:15, 4 March 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 GH6
Clan none
Mechanism inverting
Active site residues acid known, base debated
CAZy DB link
http://www.cazy.org/fam/GH6.html


Substrate specificities

Endoglucanases (EC 3.2.1.4) and cellobiohydrolases (EC 3.2.1.91)only. Both classes of enzyme active on cellulose / beta 1,4 glucans.


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 sterochemistry determination
Cite some reference here, with a short (1-2 senetence) explanation [1].
First general acid/base residue identification
Cite some reference here, with a short (1-2 senetence) explanation [2].
First 3-D structure
The catalytic core domain of the Trichoderma reesei (the organism now known as Hypocrea jecorina) cellobiohydrolase II by the Jones group [3]. The first endoglucanase in this family was the Thermomonospora fusca E2 enzyme (catalytic core) solved by the Wilson/Karplus groups[4]

References

  1. Rouvinen J, Bergfors T, Teeri T, Knowles JK, and Jones TA. (1990). Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science. 1990;249(4967):380-6. DOI:10.1126/science.2377893 | PubMed ID:2377893 [Rouvinen1990]
  2. Spezio M, Wilson DB, and Karplus PA. (1993). Crystal structure of the catalytic domain of a thermophilic endocellulase. Biochemistry. 1993;32(38):9906-16. DOI:10.1021/bi00089a006 | PubMed ID:8399160 [Spezio1993]
  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

    [4]

All Medline abstracts: PubMed