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Difference between revisions of "Glycoside Hydrolase Family 6"
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|+ Table. Putative catalytic residues of some representatives in GH family 6 (with biochemical characterization of wt and mutant enzymes). | |+ Table. Putative catalytic residues of some representatives in GH family 6 (with biochemical characterization of wt and mutant enzymes). | ||
! Proposed role | ! Proposed role | ||
Revision as of 00:02, 5 March 2010
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.
- Author: ^^^Kathleen Piens^^^ and ^^^Gideon Davies^^^
- Responsible Curator: ^^^Gideon Davies^^^
| 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.
| 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
- 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 |
- 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 |
-
Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006