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Difference between revisions of "Glycoside Hydrolase Family 97"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | Family 97 enzymes hydrolyse alpha-linked substrates; the two enzymes from this family that have been characterised to date have alpha-glucosidase (EC 3.2.1.20) and alpha-galactosidase (EC 3.2.1.22) activity <cite>REF1</cite>. The alpha-glucosidase from Bacteroides thetaiotaomicron has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing a-1,6-, a-1,3- and a-1,2-, as well as a-1,4-, linkages <cite>REF2;REF3</cite>. | |
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| − | |||
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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== References == | == References == | ||
| − | <biblio> | + | <biblio> |
| − | # | + | #REF1 pmid=18848471 |
| − | # | + | #REF2 pmid=1708385 |
| − | # | + | #REF3 pmid=18981178 |
| − | |||
</biblio> | </biblio> | ||
Revision as of 16:36, 1 October 2009
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: ^^^Tracey Gloster^^^
- Responsible Curator: ^^^Gideon Davies^^^
| Glycoside Hydrolase Family GH97 | |
| Clan | Not assigned |
| Mechanism | Retaining and Inverting |
| Active site residues | Inferred |
| CAZy DB link | |
| http://www.cazy.org/fam/GH97.html | |
Substrate specificities
Family 97 enzymes hydrolyse alpha-linked substrates; the two enzymes from this family that have been characterised to date have alpha-glucosidase (EC 3.2.1.20) and alpha-galactosidase (EC 3.2.1.22) activity [1]. The alpha-glucosidase from Bacteroides thetaiotaomicron has been characterised in the most detail, and has been demonstrated to hydrolyse substrates ranging from maltose to maltoheptaose in length, and those containing a-1,6-, a-1,3- and a-1,2-, as well as a-1,4-, linkages [2, 3].
Kinetics and Mechanism
Family GH97 is unusual as it contains both retaining and inverting enzymes. Both mechanisms are strongly dependent on the presence of calcium, which coordinates with the C2-OH group.
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 sentence) explanation [4].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [5].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [6].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [7].
References
- Gloster TM, Turkenburg JP, Potts JR, Henrissat B, and Davies GJ. (2008). Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora. Chem Biol. 2008;15(10):1058-67. DOI:10.1016/j.chembiol.2008.09.005 |
- Smith KA and Salyers AA. (1991). Characterization of a neopullulanase and an alpha-glucosidase from Bacteroides thetaiotaomicron 95-1. J Bacteriol. 1991;173(9):2962-8. DOI:10.1128/jb.173.9.2962-2968.1991 |
- Kitamura M, Okuyama M, Tanzawa F, Mori H, Kitago Y, Watanabe N, Kimura A, Tanaka I, and Yao M. (2008). Structural and functional analysis of a glycoside hydrolase family 97 enzyme from Bacteroides thetaiotaomicron. J Biol Chem. 2008;283(52):36328-37. DOI:10.1074/jbc.M806115200 |
[[Category:Glycoside Hydrolase Families|GHnnn]]