Purification and characterization of an NAD-malic enzyme from Bradyrhizobium japonicum A1017.
An NAD-malic enzyme was purified to homogeneity from Bradyrhizobium japonicum A1017, and its molecular characteristics were surveyed. The enzyme exhibited native and subunit molecular masses of 388 and 85 kDa, respectively, suggesting that it exists as a homotetramer, and was activated by metabolic intermediates in glycolysis. The role of the enzyme in bacteroids' carbon metabolism is discussed.
Chen
F
F
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Ikenobe 2393, Kita-gun, Kagawa 761-07, Japan.
Okabe
Y
Y
Osano
K
K
Tajima
S
S
D000595:Amino Acid Sequence; D020369:Bradyrhizobium / Q000201:enzymology*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D007700:Kinetics; D046911:Macromolecular Substances; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D013379:Substrate Specificity
D046911:Macromolecular Substances; D010446:Peptide Fragments; D008291:Malate Dehydrogenase; C046446:malate dehydrogenase-(oxaloacetate-decarboxylating) (NAD+)