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Difference between revisions of "Glycoside Hydrolase Family 6"
| Line 28: | Line 28: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | [[ | + | [[Glycoside hydrolases]] of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC [{{EClink}}3.2.1.4 3.2.1.4]) and cellobiohydrolase (EC [{{EClink}}3.2.1.91 3.2.1.91]) activity has been reported for both bacterial and eukaryotic members of this family. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| Line 91: | Line 91: | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 senetence) explanation | + | ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 senetence) explanation. |
| − | ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation | + | ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 senetence) explanation. |
;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 <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite> | ;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 <cite>Rouvinen1990</cite>. The first endoglucanase in this family was the ''Thermomonospora fusca'' E2 enzyme (catalytic core) solved by the Wilson/Karplus groups<cite>Spezio1993</cite> | ||
| Line 101: | Line 101: | ||
#Rouvinen1990 pmid=2377893 | #Rouvinen1990 pmid=2377893 | ||
#Spezio1993 pmid=8399160 | #Spezio1993 pmid=8399160 | ||
| − | + | ||
| − | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH006]] | [[Category:Glycoside Hydrolase Families|GH006]] | ||
Revision as of 07:21, 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
Glycoside hydrolases of family 6 cleave β-1,4 glycosidic bonds in cellulose/β-1,4-glucans. Only endoglucanase (EC 3.2.1.4) and cellobiohydrolase (EC 3.2.1.91) activity has been reported for both bacterial and eukaryotic members of this family.
Kinetics and Mechanism
Family 6 enzymes are inverting enzymes, as first shown by NMR [1] on Cellobiohydrolase II (CBH II; Cel6A) from the fungus Trichoderma reesei (a clonal derivative of Hypocrea jecorina [2]).
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.
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 senetence) explanation.
- 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
-
Knowles, J.K.C., Lehtovaara, P., Murray, M. and Sinnott, M.L. (1988) Stereochemical course of the action of the cellobioside hydrolases I and II of Trichoderma reesei. J. Chem. Soc., Chem. Commun., 1988, 1401-1402. DOI: 10.1039/C39880001401
- Kuhls K, Lieckfeldt E, Samuels GJ, Kovacs W, Meyer W, Petrini O, Gams W, Börner T, and Kubicek CP. (1996). Molecular evidence that the asexual industrial fungus Trichoderma reesei is a clonal derivative of the ascomycete Hypocrea jecorina. Proc Natl Acad Sci U S A. 1996;93(15):7755-60. DOI:10.1073/pnas.93.15.7755 |
- 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 |