Paper
Hydrolytic Activity of α-Mannosidase against Deoxy Derivatives of p-Nitrophenyl α-d-Mannopyranoside
Published Dec 23, 1996 · T. Nishio, Y. Miyake, Hitomi Tsujii
Bioscience, Biotechnology, and Biochemistry
22
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1
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Abstract
Deoxy derivatives of p-nitrophenyl (PNP) α-d-mannopyranoside, PNP 2-deoxy-α-d-arabino-hexopyranoside, 3-deoxy-α-d-arabino-hexopyranoside, 4-deoxy-α-d-lyxo-hexopyranoside, and α-d-rhamnopyranoside, were synthesized and hydrolytic activities of jack bean and almond α-mannosidases against them were investigated. These α-mannosidases scarcely acted on the 2-, 3-, and 4-deoxy derivatives, while the 6-deoxy one was hydrolyzed by the enzymes as fast as PNP α-d-mannopyranoside, which is a common substrate for α-mannosidase. These results indicate that the hydroxyl groups at C-2, 3, and 4 of the mannopyranoside are necessary to be recognized as a substrate by these enzymes, while that at C-6 does not have so a crucial role in substrate discrimination. Values of Km and Vmax of the enzymes on the hydrolysis of PNP α-d-rhamnopyranoside were obtained from kinetic studies.
-mannosidase mainly hydrolyzes 6-deoxy p-nitrophenyl -d-mannopyranoside, while 2-, 3-, and 4-deoxy derivatives show limited activity, suggesting hydroxyl groups at C-2, 3, and 4 are crucial for substrate recognition.
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