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Microbiology 142 (1996), 2631-2634
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microbiology, Vol 142, 2631-2634, Copyright © 1996 by Society for General Microbiology

ARTICLES

Adenosylcobalamin-dependent methylmalonyl-CoA mutase isozymes in the photosynthetic protozoon Euglena gracilis Z

F Watanabe, K Abe, Y Tamura and Y Nakano
Department of Food and Nutrition, Kochi Women's University, Japan. watanabe@cc.kochi-wu.ac.jp

The photosynthetic protozoon Euglena gracilis Z contains adenosylcobalamin-dependent methylmalonyl-CoA mutase (MCM) involved in propionate metabolism. The specific activity of the Euglena mutase was about 6.5-fold greater in propionate-adapted Euglena cells than in photoautotrophic cells (control). Although the control cells contained only one mutase (apparent M(r) 72,000), the propionate-adapted cells contained two mutases with M(r) values of 72,000 and 17,000; both enzymes were located in the mitochondria. These results provide evidence that propionate-adapted Euglena contains two MCM isozymes. The induced mutase (M(r) 17,000) permits photoassimilation of propionate.


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