Plant Physiology 51:492-503 (1973)
© 1973 American Society of Plant Biologists
Articles
-Cystathionase In Vivo Inactivation by Rhizobitoxine and Role of the Enzyme in Methionine Biosynthesis in Corn Seedlings
John Giovanelli,
Lowell D. Owens1 and
S. Harvey Mudd
Laboratory of General and Comparative Biochemistry, National Institutes of Mental Health, Bethesda, Maryland 20014,
United States Soils Laboratory, Soil and Water Conservation Research Division, Agriculture Research Service, United States Department of Agriculture, Beltsville, Maryland 20705
Rhizobitoxine has previously been shown to inactivate irreversibly -cystathionase isolated from spinach. In the present studies, rhizobitoxine was shown to inhibit partially -cystathionase of spinach and corn seedlings in vivo. An activity of 30 to 40% of normal remained in toxin-treated seedlings of both spinach and corn. Possible reasons for the partial inhibition are discussed.
Rhizobitoxine-treated and control corn seedlings were allowed to assimilate 35SO42 for 3 or 6 hours, and the radioactivity incorporated into sulfur amino acids at these times was studied. The most striking effect of rhizobitoxine was an increase (up to 22-fold) in radioactive cystathionine. Accumulation of radioactivity in methionine was only slightly inhibited by rhizobitoxine treatment. The results strongly suggest that the transsulfuration pathway contributes to methionine biosynthesis, and that metabolism via this pathway is impaired, but not entirely eliminated, by rhizobitoxine treatment.
The present data do not permit decisions about the relative contributions of the transsulfuration and the direct sulfhydration pathways to methionine biosynthesis, or whether the pathological effects of rhizobitoxine are due chiefly to inhibition of -cystathionase.
1 Present address: South Carolina State College, Post Office Box 1706, Orangeburg, S. C. 29115.
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