Purification and characterization of the NADP-malic enzyme from Bradyrhizobium japonicum A1017.
An NADP-malic enzyme [EC 1.1.1.40] was purified to homogeneity from Bradyrhizobium japonicum A1017, and the molecular and physiological characteristics were surveyed. The molecular mass of one subunit of the purified enzyme was evaluated to be 77,600 Da by SDS-PAGE, and the native enzyme was a tetramer in pH 7.0 and dimer in pH 8.0 conditions, showing complex oligomeric characteristics corresponding to pH value.
Chen
F
F
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
Okabe
Y
Y
Osano
K
K
Tajima
S
S
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D012230:Rhizobiaceae / Q000201:enzymology*
D001426:Bacterial Proteins; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)