Plant Physiol.
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Plant Physiology 94:67-70 (1990)
© 1990 American Society of Plant Biologists

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Metabolism and Enzymology

A Higher Plant Enzyme Exhibiting Broad Acceptance of Stereoisomers 1

Denise Kavanaugh, Milan A. Berge and Gerald A. Rosenthal

The Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40506, The T. H. Morgan School of Biological Sciences, University of Kentucky, Lexington, Kentucky 40506

An arginase, purified from the leaf of the jack bean, Canavalia ensiformis, can effectively hydrolyze both L- and D-arginine. Arginases, examined from a number of other plant and animal sources, exhibit marked substrate stereospecificity and fail to catabolize D-arginine. In order to provide essential nitrogen, jack bean leaf arginase also catabolizes L-canavanine, an arginine analog that is a predominant nitrogen-storing metabolite of this legume. The ability of arginase to metabolize both stereoisomers of arginine may result from the requirement for this enzyme to exhibit limited substrate specificity in order to hydrolyze both arginine and canavanine.

1 The authors acknowledge gratefully support by the National Science Foundation (DCB-8901749), National Institutes of Health Biomedical Research Grant (2-S07-RR07114-21), the Graduate School of the University of Kentucky, and the Department of Education Minority Participation in Graduate Education Program.




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C. Melangeli, G. A. Rosenthal, and D. L. Dalman
The biochemical basis for L-canavanine tolerance by the tobacco budworm Heliothis virescens (Noctuidae)
PNAS, March 18, 1997; 94(6): 2255 - 2260.
[Abstract] [Full Text] [PDF]


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Copyright © 1990 by the American Society of Plant Biologists