Plant Physiology 71:551-554 (1983)
© 1983 American Society of Plant Biologists
Articles
Mechanism of Inhibition of Jack Bean -Mannosidase by Swainsonine 1
Mohinder S. Kang2 and
Alan D. Elbein
Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick, Maryland 21701,
Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78284
The indolizidine alkaloid, swainsonine, was previously shown to be a potent inhibitor of lysosomal and jack bean -mannosidase (Dorling, Huxtable, Colegate 1980 Biochem J 191: 649-651). We examined the effects of various concentrations of this alkaloid on a number of commercially available glycosidases and found swainsonine to be quite specific for -mannosidase (50% inhibition at 1-5 x 107 molar). Optimum inhibition was observed after a 2-minute preincubation of enzyme and inhibitor. Lineweaver-Burk plots of substrate concentration versus velocity in the presence of various amounts of swainsonine showed considerable curvature at high substrate concentrations, suggesting that swainsonine may be a competitive inhibitor that binds tightly to the enzyme and is only slowly removed. Periodate oxidation of swainsonine completely destroyed its inhibitory activity.
2 Present Address: National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, MD 20205.
1 Supported by grants from the National Institutes of Health (AM 21800 and HL 17783).
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