Substrate Selectivity inAspergillus nigerKU-8 Acid Phosphatase II Using Phosphoryl Oligosaccharides | Zendy

Kenji To-o | Zendy; Hiroshi Kamasaka | Zendy; Takashi Kuriki | Zendy; Shigetaka Okada | Zendy

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Substrate Selectivity inAspergillus nigerKU-8 Acid Phosphatase II Using Phosphoryl Oligosaccharides

Author(s) -

Kenji To-o,

Hiroshi Kamasaka,

Takashi Kuriki,

Shigetaka Okada

Publication year - 2000

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.64.1534

Subject(s) - maltotriose , aspergillus niger , phosphatase , chemistry , substrate (aquarium) , phosphate , stereochemistry , acid phosphatase , enzyme , biochemistry , maltose , biology , ecology

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.

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