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Difference between revisions of "Glycoside Hydrolase Family 77"
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== Substrate specificities == | == Substrate specificities == | ||
[[Glycoside hydrolase]] family 77 is the member of the α-amylase clan [[GH-H]] <cite>Cantarel2009</cite>, together with [[GH13]] and [[GH70]] <cite>MacGregor2001</cite>. The family contains only one enzyme specificity - the amylomaltase (EC [{{EClink}}2.4.1.25 2.4.1.25]), that is known as disproportionating enzyme (D-enzyme) <cite>Takaha1993<cite> in plants or 4-α-glucanotransferase in bacteria <cite>Terada1999<cite> and archaeons <cite>Kaper2005<cite>. | [[Glycoside hydrolase]] family 77 is the member of the α-amylase clan [[GH-H]] <cite>Cantarel2009</cite>, together with [[GH13]] and [[GH70]] <cite>MacGregor2001</cite>. The family contains only one enzyme specificity - the amylomaltase (EC [{{EClink}}2.4.1.25 2.4.1.25]), that is known as disproportionating enzyme (D-enzyme) <cite>Takaha1993<cite> in plants or 4-α-glucanotransferase in bacteria <cite>Terada1999<cite> and archaeons <cite>Kaper2005<cite>. | ||
| + | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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#Terada1999 pmid=10049841 | #Terada1999 pmid=10049841 | ||
#Kaper2005 pmid=16151092 | #Kaper2005 pmid=16151092 | ||
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</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH077]] | [[Category:Glycoside Hydrolase Families|GH077]] | ||
Revision as of 00:18, 16 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.
- Author: ^^^Stefan Janecek^^^
- Responsible Curator: ^^^Stefan Janecek^^^
| Glycoside Hydrolase Family GH77 | |
| Clan | GH-H |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/fam/GH77.html | |
Substrate specificities
Glycoside hydrolase family 77 is the member of the α-amylase clan GH-H [1], together with GH13 and GH70 [2]. The family contains only one enzyme specificity - the amylomaltase (EC 2.4.1.25), that is known as disproportionating enzyme (D-enzyme) Takaha1993 in plants or 4-α-glucanotransferase in bacteria Terada1999 and archaeons Kaper2005.
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation.
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation.
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation.
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation.
References
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
- MacGregor EA, Janecek S, and Svensson B. (2001). Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta. 2001;1546(1):1-20. DOI:10.1016/s0167-4838(00)00302-2 |
- Takaha T, Yanase M, Okada S, and Smith SM. (1993). Disproportionating enzyme (4-alpha-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J Biol Chem. 1993;268(2):1391-6. | Google Books | Open Library
- Terada Y, Fujii K, Takaha T, and Okada S. (1999). Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose. Appl Environ Microbiol. 1999;65(3):910-5. DOI:10.1128/AEM.65.3.910-915.1999 |
- Kaper T, Talik B, Ettema TJ, Bos H, van der Maarel MJ, and Dijkhuizen L. (2005). Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels. Appl Environ Microbiol. 2005;71(9):5098-106. DOI:10.1128/AEM.71.9.5098-5106.2005 |