Glycoside Hydrolase Family 77

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• Author: ^^^Stefan Janecek^^^
• Responsible Curator: ^^^Stefan Janecek^^^

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Glycoside Hydrolase Family GH77
Clan	GH-H
Mechanism	retaining
Active site residues	known
CAZy DB link
https://www.cazy.org/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) in plants [3] or 4-α-glucanotransferase in bacteria [4] and archaeons [5]. As of April 2010, it has more than 700 members [1] with more than 650 from Bacteria, ~10 from Archaea and a few tens from Eukarya (plants and green algae).

Amylomaltase catalyses the glucan-chain transfer from one α-1,4-glucan to another α-1,4-glucan (or to 4-hydroxyl group of glucose) or within a single linear glucan molecule to produce a cyclic α-1,4-glucan with degree of polymerization starting from 17 [3, 4, 5]. Cyclodextrin glucanotransferase, a member of the α-amylase family GH13, also produces cyclic α-1,4-glucans, but with a small degree of polymerization (6-8), called cyclodextrins [6].

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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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 |
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 |