Glycosidases: a key to tailored carbohydrates
In recent years, carbohydrate-processing enzymes have become the enzymes of choice in many applications thanks to their stereoselectivity and efficiency. This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with en...
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| Veröffentlicht in: | Trends in biotechnology (Regular ed.) 2009-04, Vol.27 (4), p.199-209 |
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| creator | BOJAROVA, Pavla KREN, Vladimir |
| description | In recent years, carbohydrate-processing enzymes have become the enzymes of choice in many applications thanks to their stereoselectivity and efficiency. This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with engineered substrates, and mutant glycosidases. Genetic engineering has recently produced glucuronyl synthases, an inverting xylosynthase and the first mutant endo -β- N -acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N -acetyl-β-galactosaminuronates, β1,4-linked mannosides and α1,4-linked galactosides. The efficient selection of mutant enzymes is facilitated by high-throughput screening assays involving the co-expression of coupled enzymes or chemical complementation. Selective glycosidase inhibitors and highly specific glycosidases are finding attractive applications in biomedicine, biology and proteomics. |
| doi_str_mv | 10.1016/j.tibtech.2008.12.003 |
| format | Article |
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Selective glycosidase inhibitors and highly specific glycosidases are finding attractive applications in biomedicine, biology and proteomics.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carbohydrate Metabolism</subject><subject>Carbohydrates</subject><subject>Carbohydrates - biosynthesis</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>Enzymes</subject><subject>Fluorides</subject><subject>Fundamental and applied biological sciences. 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This review presents recent developments in glycosidase-catalyzed synthesis via two complementary approaches: the use of wild-type enzymes with engineered substrates, and mutant glycosidases. Genetic engineering has recently produced glucuronyl synthases, an inverting xylosynthase and the first mutant endo -β- N -acetylglucosaminidase. A thorough selection of enzyme strains and aptly modified substrates have resulted in rare glycostructures, such as N -acetyl-β-galactosaminuronates, β1,4-linked mannosides and α1,4-linked galactosides. The efficient selection of mutant enzymes is facilitated by high-throughput screening assays involving the co-expression of coupled enzymes or chemical complementation. Selective glycosidase inhibitors and highly specific glycosidases are finding attractive applications in biomedicine, biology and proteomics.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Ltd</pub><pmid>19250692</pmid><doi>10.1016/j.tibtech.2008.12.003</doi><tpages>11</tpages></addata></record> |
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| ispartof | Trends in biotechnology (Regular ed.), 2009-04, Vol.27 (4), p.199-209 |
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| subjects | Biological and medical sciences Biotechnology Carbohydrate Metabolism Carbohydrates Carbohydrates - biosynthesis Catalysis Chemistry Enzymes Fluorides Fundamental and applied biological sciences. Psychology Genetic engineering Glycoside Hydrolases - antagonists & inhibitors Glycoside Hydrolases - genetics Glycoside Hydrolases - metabolism Internal Medicine Mutant Proteins - metabolism Protein Engineering Proteomics Substrate Specificity |
| title | Glycosidases: a key to tailored carbohydrates |
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