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Glycoside Hydrolase Family 6

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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.



Table. Putative catalytic residues of some representatives in GH family 6 (with biochemical characterization of wt and mutant enzymes).
Proposed role CfCel6A (endo) HiCel6A (exo) HjCel6A (exo) TfCel6A (endo) TfCel6B (exo)
Substrate distortion Asp210 Tyr174 Tyr169 Tyr73 Tyr220
Increase in pKa acid/Catalytic base Asp216 Asp180 Asp175 Asp79 Asp226
Proton network Gly222 Ser186 Ser181 Ser85 Asp232
Catalytic acid Asp252 Asp226 Asp221 Asp117 Asp274
Catalytic base/substrate binding Asp392 Asp405 Asp401 Asp265 Asp497


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