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Difference between revisions of "Glycoside Hydrolase Family 91"
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Entries in [[Glycoside Hydrolase Family 91]] were reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]). | Entries in [[Glycoside Hydrolase Family 91]] were reclassified to [[Polysaccharide Lyase Family 19]] on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC [{{EClink}}4.2.2.17 4.2.2.17] and EC [{{EClink}}4.2.2.18 4.2.2.18]). | ||
| − | The family was '' | + | The family was ''placed back'' to [[Glycoside Hydrolase Family 91]] on 20 April 2010 due to direct analogy with the lytic transglycosidases of [[GH23]], [[GH102]], [[GH103]], and [[GH104]] and in particular the observation of a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) in this family <cite>Sakurai1997 Saito2003</cite>. |
== Substrate specificities == | == Substrate specificities == | ||
Revision as of 00:54, 20 April 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.
- Temporary Responsible Curator: ^^^Bernard Henrissat^^^
| Glycoside Hydrolase Family GH91 | |
| Clan | |
| Mechanism | |
| Active site residues | |
| CAZy DB link | |
| http://www.cazy.org/fam/GH91.html | |
History of reclassification
Entries in Glycoside Hydrolase Family 91 were reclassified to Polysaccharide Lyase Family 19 on 30 July 2008 due to recommendations of the NC-IUBMB, which stated that these enzymes are lyases, as there is no water involved in the reaction. Indeed, polysaccharide cleavage in some members occurs via intramolecular hydroxide attack, rather than glycosidic bond hydrolysis (see EC 4.2.2.17 and EC 4.2.2.18).
The family was placed back to Glycoside Hydrolase Family 91 on 20 April 2010 due to direct analogy with the lytic transglycosidases of GH23, GH102, GH103, and GH104 and in particular the observation of a hydrolase (di-fructofuranose 1,2':2,3' dianhydride hydrolase, DFA-IIIase) in this family [1, 2].
Substrate specificities
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Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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References
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H. Sakurai, A. Yokota, Y. Sumita, Y. Mori, H. Matsui and F. Tomita, Metabolism of DFA III by Arthrobacter sp. H65-7: purification and properties of a DFA III hydrolysis enzyme (DFA IIIase). Biosci. Biotechnol. Biochem. 61 (1997), pp. 989–993. DOI: 10.1271/bbb.61.989
- Saito K, Sumita Y, Nagasaka Y, Tomita F, and Yokota A. (2003). Molecular cloning of the gene encoding the di-D-Fructofuranose 1,2':2,3' dianhydride hydrolysis enzyme (DFA IIIase) from Arthrobacter sp. H65-7. J Biosci Bioeng. 2003;95(5):538-40. DOI:10.1016/s1389-1723(03)80058-0 |