Adenosylcobalamin-dependent methylmalonyl-CoA mutase isozymes in the photosynthetic protozoon Euglena gracilis Z.
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.
Watanabe
F
F
Department of Food and Nutrition, Kochi Women's University, Japan. watanabe@cc.kochi-wu.ac.jp
Abe
K
K
Tamura
Y
Y
Nakano
Y
Y
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005056:Euglena gracilis / Q000201:enzymology*; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008765:Methylmalonyl-CoA Mutase / Q000302:isolation & purification / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D011422:Propionates / Q000378:metabolism
D007527:Isoenzymes; D011422:Propionates; D008765:Methylmalonyl-CoA Mutase