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Microbiology 142 (1996), 2631-2634; DOI  10.1099/00221287-142-9-2631
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Adenosylcobalamin-dependent methylmalonyl-CoA mutase isozymes in the photosynthetic protozoon Euglena gracilis Z

Fumio Watanabe1,4, Katsuo Abe1, Yoshiyuki Tamura2 and Yoshihisa Nakano3

Department of Food and Nutrition, Kochi Women's University, Kochi 780, Japan
Laboratory of Nutrition and Food Science, Hagoromo-gakuen College, Sakai, Osaka 592, Japan
Department of Applied Biological Chemistry, Osaka Prefecture University, Sakai, Osaka 593, Japan

4Author for correspondence: Fumio Watanabe. Tel/Fax: +81 888 31 2876. e-mail: watanabe@cc.kochi-wu.ac.jp

ABSTRACT

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 Mr 72000), the propionate-adapted cells contained two mutases with Mr values of 72000 and 17000; both enzymes were located in the mitochondria. These results provide evidence that propionate-adapted Euglena contains two MCM isozymes. The induced mutase (Mr 17000) permits photoassimilation of propionate.

Keywords: propionate metabolism, adenosylcobalamin, methylmalonyl-CoA mutase, mitochondria, Euglena gracilis Z




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