[Physicochemical, catalytic, and regulatory properties of malate dehydrogenase from Rhodovulum steppense bacteria, strain A-20s].
The physicochemical, regulatory, and kinetic properties of malate dehydrogenase (EC 1.1.1.37) from haloalkaliphilic purple nonsulfur Rhodovulum steppense bacteria, strain A-20s, were studied. The malate dehydrogenase (MDH) preparation with a specific activity of 0.775 ± 0.113 U/mg protein was obtained in an electrophoretically homogeneous state using multistep purification. Using homogenous preparations, the molecular weight and the Michaelis constant of the enzyme were determined; the effects of metal ions, the temperature effect, and the thermal stability of the MDH were studied. The dimer structure of the enzyme was demonstrated by DS-Na-electrophoresis.
A T
AT
Eprintsev
M I
MI
Falaleeva
I V
IV
Parfenova
M S
MS
Liashchenko
E I
EI
Kompantseva
A Iu
AIu
Tret'iakova
D000222:Adaptation, Physiological; D020134:Catalytic Domain; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D011487:Protein Conformation; D041903:Rhodovulum / Q000201:enzymology* / Q000502:physiology; D013379:Substrate Specificity; D013696:Temperature
D004791:Enzyme Inhibitors; D008291:Malate Dehydrogenase