1. In order to elucidate the location of chorismate mutase and prephenate dehydrogenase on E. coli T-protein, protein limited digestion and fragmentation cloning were employed.

2. Prosthetic enzyme of mutase, catalyze reactions of group, mainly methyl, metachoresis in the interior of substrate molecule.

3. T-protein from Escherichia coli consists of three domains:chorismate mutase, prephenate dehydrogenase and a regulatory domain.

4. The hydrogen peroxide eliminates by the catalase and the peroxide enzyme, the oxygen free eliminates fragrant by the hyperoxide mutase.

5. In a conclusion, E. coli T-protein do have independent domains, N-terminal 93 amino acids belongs to chorismate mutase and C-terminal 277 amino acids belongs to prephenate dehydrogenase.

6. Methylmalonic acidemia is an inherited metabolic disorder, which is caused by deficiency of methylmalonyl-coenzyme A mutase or its cofactor adenosylcobalamin.