Substrate Selectivity inAspergillus nigerKU-8 Acid Phosphatase II Using Phosphoryl Oligosaccharides
| Autor: | Shigetaka Okada, Kenji To-O, Takashi Kuriki, Hiroshi Kamasaka |
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| Rok vydání: | 2000 |
| Předmět: |
inorganic chemicals
Phosphoric monoester hydrolases Acid Phosphatase macromolecular substances environment and public health Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Analytical Chemistry chemistry.chemical_compound Maltotriose Molecular Biology chemistry.chemical_classification biology Organic Chemistry Aspergillus niger Acid phosphatase Substrate (chemistry) General Medicine biology.organism_classification Phosphate enzymes and coenzymes (carbohydrates) Enzyme chemistry biology.protein bacteria Selectivity Trisaccharides Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 64:1534-1537 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.64.1534 |
| Popis: | The intracellular acid phosphatase II (ACPase II) produced by Aspergillus niger KU-8 preferentially dephosphorylates C-6 phosphate groups rather than C-3 phosphate groups of phosphoryl oligosaccharides. In this study, the kinetic parameters of ACPase II were measured. 3(2)-phosphoryl maltotriose and 6(2)-phosphoryl maltotriose, which differ only in the binding position of the phosphate group, were prepared and used as the substrates. The Km for both substrates were similar. However, the k(cat) value for the 6(2)-phosphoryl maltotriose was about three-fold of that for the 3(2)-phosphoryl maltotriose. |
| Databáze: | OpenAIRE |
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