Glycoside hydrolase family 33
| Sialidase, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| Symbol | Sialidase | ||||||||
| Pfam | PF02973 | ||||||||
| InterPro | IPR004124 | ||||||||
| SCOP | 1sli | ||||||||
| SUPERFAMILY | 1sli | ||||||||
| CAZy | GH33 | ||||||||
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In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]
This family contains sialidases (CAZY GH_33), which hydrolyse alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Sialidases may act as pathogenic factors in microbial infections.[6] The 1.8 A structure of trans-sialidase from leech (Macrobdella decora, Q27701) in complex with 2-deoxy-2, 3-didehydro-NeuAc was solved. The refined model comprising residues 81-769 has a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain.[7]
References
- ↑ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. PMC 41477
. PMID 7624375. doi:10.1073/pnas.92.15.7090. - ↑ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. PMID 8535779. doi:10.1016/S0969-2126(01)00220-9.
- ↑ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ↑ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ↑ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
- ↑ Rothe B, Rothe B, Roggentin P, Schauer R (1991). "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins". Mol. Gen. Genet. 226 (1–2): 190–197. PMID 2034213. doi:10.1007/BF00273603.
- ↑ Luo M, Luo Y, Li SC, Chou MY, Li YT (1998). "The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity". Structure. 6 (4): 521–530. PMID 9562562. doi:10.1016/S0969-2126(98)00053-7.