Hydrolytic Activity ofα-Mannosidase against Deoxy Derivatives ofp-Nitrophenylα-d-Mannopyranoside
- 1 January 1996
- journal article
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 60 (12) , 2038-2042
- https://doi.org/10.1271/bbb.60.2038
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.Keywords
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