2002 Volume 48 Issue 3 Pages 242-246
Summary High activity (about 50 mU⋅mg protein-1) of methylmalonyl-CoA mutase (82-95% apo-enzyme) was constantly found during the cell growth of a methanol-utilizing bacterium, Methylobacterium extorquens NR-1. The apo-enzyme was purified to homogeneity and characterized. The purified enzyme was colorless. An apparent Mr of M. extorquens NR-1 enzyme was calculated to be 150, 000±5, 000 by Superdex 200 HR gel filtration. SDS-polyacrylamide gel electrophoresis of the purified enzyme gave two protein bands with an apparent Mr of 85, 000±2, 000 and 70, 000±2, 000, indicating that the M. extorquens NR-1 enzyme is composed of two nonidentical subunits. NH2-terminal amino acid sequences of the small and large subunits of M. extorquens NR-1 enzyme showed no significant homology to those of the enzyme from other species. Some enzymological properties of the M, extorquens NR-1 enzyme were studied.
