NAD-DEPENDENT FORMATE DEHYDROGENASE FROM METHYLOTROPHIC BACTERIUM PSEUDOMONAS sp. 101. I. AMINO ACID SEQUENCE
V. O. POPOV, I. A. SHUMILIN, T. B. USTINNIKOVA, V. S. LAMZIN, Ts. A. EGOROV*
A. N. Bach Institute of Biochemistry, Academy of Sciences of the USSR, Moscow' *N. I. Vavilov Institute of General Genetics, Academy of Sciences of the USSR, Moscow
Abstract: The primary structure of NAD-dependent formate dehydrogenase from methylotrop-hic bacterium Pseudomonas sp. 101 is determined. The enzyme is composed of two identical subunits, each comprising 393 amino acid residues, and has a molecular weight of 43.1 kD. To elucidate the protein's amino acid sequence, four types of digestion were used: cyanogen bromide cleavage at methionine residues, endoproteinase Lys-C digestion at lysine residues, endoproteinase Glu-C cleavage at glutamic acid residues, and tryptic digestion. The peptides obtained were purified to homogeneity and characterized.
Russian Journal of Bioorganic Chemistry 1990, 16 (3):324-335