[Structural-functional transformation of the malate dehydrogenase system of the bacterium Sphaerotilus sp. strain D-507 depending on nutritional mode].
High-purity preparations of malate dehydrogenase (EC 1.1.1.37) were obtained by multistage purification from the bacterium Sphaerotilus sp. strain D-507 growing under different conditions. Under organotrophic conditions, the enzyme was dimeric; under mixotrophic conditions, dimeric and trimeric. On the basis of studied properties of the enzyme preparations, data on the activity of enzymes of the glyoxylate and tricarboxylic-acid cycles, and analysis of published data, it can be concluded that malate dehydrogenase isoforms are implicated in the adaptive response of bacteria to changing culturing conditions.
Eprintsev
A T
AT
Falaleeva
M I
MI
Arabtseva
M A
MA
Parfenova
I V
IV
D000220:Adaptation, Biological / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002952:Citric Acid Cycle / Q000502:physiology; D006038:Glyoxylates / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D042744:Sphaerotilus / Q000201:enzymology* / Q000254:growth & development*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D006038:Glyoxylates; D007527:Isoenzymes; D008291:Malate Dehydrogenase; C031150:glyoxylic acid