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

Microbiology (Reading). 1996 Sep:142 ( Pt 9):2631-4. doi: 10.1099/00221287-142-9-2631.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, High Pressure Liquid
  • Euglena gracilis / enzymology*
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism*
  • Methylmalonyl-CoA Mutase / isolation & purification
  • Methylmalonyl-CoA Mutase / metabolism*
  • Mitochondria / enzymology
  • Propionates / metabolism

Substances

  • Isoenzymes
  • Propionates
  • Methylmalonyl-CoA Mutase