Optimum Substrate Size and Specific Anomer Requirements for the Reducing-End Glycoside Hydrolase Di-N-Acetylchitobiase
| Autor: | Nathan N. Aronson, Brian A. Halloran |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Anomer
Stereochemistry Trimer Chitobiose Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Analytical Chemistry chemistry.chemical_compound Acetylglucosaminidase Animals Humans Monosaccharide Glycosyl Glycoside hydrolase Molecular Biology chemistry.chemical_classification Hydrolysis Organic Chemistry Substrate (chemistry) Glycoside General Medicine Recombinant Proteins carbohydrates (lipids) Kinetics Carbohydrate Sequence chemistry Chickens Oxidation-Reduction Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 70:1537-1541 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.60183 |
| Popis: | Di-N-acetylchitobiase is a family 18 glycoside hydrolase that splits the reducing-end GlcNAc from chitooligosaccharides. The enzyme hydrolyzed only the alpha-anomer of five tested substrates, chitin di- through hexasaccharide. In all cases the glycosyl fragment retained its beta-configuration while the split monosaccharide was alpha-D-GlcNAc. Chitobiose was hydrolyzed less than half as fast as the other larger substrates. All four of them, tri- to hexasaccharide, reacted at the same rate. The biochemical behavior of di-N-acetylchitobiase indicates it has three subsites, -2, -1, +1, in which the reducing-end trimer of any sized chitooligosaccharide is bound. The +1 site is specific for an alpha-anomer. |
| Databáze: | OpenAIRE |
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