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Glycoside Hydrolase Family 77

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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.


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

  1. 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 | PubMed ID:18838391 [Cantarel2009]
  2. 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 | PubMed ID:11257505 [MacGregor2001]
  3. 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 PubMed ID:7678257 [Takaha1999]
  4. 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 | PubMed ID:10049841 [Terada1999]
  5. 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 | PubMed ID:16151092 [Kaper2005]

All Medline abstracts: PubMed