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Glycoside hydrolase family 33

In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases.

Glycoside hydrolases 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. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.

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. The 1.8 A structure of trans-sialidase from leech (Macrobdella decora, ) 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.

References

References

  1. (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America.
  2. (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure.
  3. (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal.
  4. "Home".
  5. (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research.
  6. "Glycoside Hydrolase Family 33".
  7. (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes". Glycobiology.
  8. (April 1991). "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins". Molecular & General Genetics.
  9. (April 1998). "The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity". Structure.
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