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

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 |
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
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 |
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 |
6. Leemhuis H, Kelly RM, and Dijkhuizen L. (2010). Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications. Appl Microbiol Biotechnol. 2010;85(4):823-35. DOI:10.1007/s00253-009-2221-3 |
7. Godány A, Vidová B, and Janecek S. (2008). The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved. FEMS Microbiol Lett. 2008;284(1):84-91. DOI:10.1111/j.1574-6968.2008.01191.x |
8. Przylas I, Tomoo K, Terada Y, Takaha T, Fujii K, Saenger W, and Sträter N. (2000). Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans. J Mol Biol. 2000;296(3):873-86. DOI:10.1006/jmbi.1999.3503 |
8. Przylas I, Terada Y, Fujii K, Takaha T, Saenger W, and Sträter N. (2000). X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans. Eur J Biochem. 2000;267(23):6903-13. DOI:10.1046/j.1432-1033.2000.01790.x |
9. Srisimarat W, Murakami S, Pongsawasdi P, and Krusong K. (2013). Crystallization and preliminary X-ray crystallographic analysis of the amylomaltase from Corynebacterium glutamicum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013;69(Pt 9):1004-6. DOI:10.1107/S1744309113020319 |
10. Hoon-Hanks LL, Morton EA, Lybecker MC, Battisti JM, Samuels DS, and Drecktrah D. (2012). Borrelia burgdorferi malQ mutants utilize disaccharides and traverse the enzootic cycle. FEMS Immunol Med Microbiol. 2012;66(2):157-65. DOI:10.1111/j.1574-695X.2012.00996.x |
11. Jung JH, Jung TY, Seo DH, Yoon SM, Choi HC, Park BC, Park CS, and Woo EJ. (2011). Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus. Proteins. 2011;79(2):633-44. DOI:10.1002/prot.22911 |
12. van der Maarel MJ and Leemhuis H. (2013). Starch modification with microbial alpha-glucanotransferase enzymes. Carbohydr Polym. 2013;93(1):116-21. DOI:10.1016/j.carbpol.2012.01.065 |