Homoserine Dehydrogenase of Rhodospirillum rubrum. Physical and Chemical Characterization
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Homoserine Dehydrogenase of Rhodospirillum rubrum
Homoserine dehydrogenase catalyzes the reductive conversion of aspartate P-semialdehyde to homoserine (l), which has been identified in several microorganisms as a precursor of three other amino acids. On the one hand, homoserine is converted to methionine, and through a separate sequence of reactions is transformed to threonine, a precursor of isoleucine (2). Recent studies (3-7) have provided...
متن کاملHomoserine Dehydrsgenase of Rhodospirillum rubrum
Homoserine dehydrogenase of Rhodospirillum rubrum has been purified by heat treatment, ammonium sulfate fractionation, and by two successive gel filtration steps on Sephadex G-ZOO in the absence and presence of L-threonine, an allosteric inhibitor. The pure protein is free of aspartokinase and aspartate /?-semialdehyde dehydrogenase activities. From the sedimentation velocity centrifugation and...
متن کاملCarbon monoxide dehydrogenase from Rhodospirillum rubrum.
The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis. In vitro, this enzyme catalyzed a two-electron oxidation of CO to form CO2 as the product. The reaction was dependent on the addition of an electron accept...
متن کاملThe succinic dehydrogenase from Rhodospirillum rubrum.
Succinic dehydrogenase has usually been associated with a macromolecular intracellular unit (mitochondria) whenever the enzyme has been isolated. In an ultracentrifugal analysis of the composition of extracts of various organisms, Schachman et al. (1952) found that Rhodospirillum rubrum yielded particles with a wide range of sedimentation constants. Succinic dehydrogenase has been demonstrated ...
متن کاملRedox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum.
Studies of initial activities of carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum show that CODH is mostly inactive at redox potentials higher than -300 mV. Initial activities measured at a wide range of redox potentials (0--500 mV) fit a function corresponding to the Nernst equation with a midpoint potential of -316 mV. Previously, extensive EPR studies of CODH have suggested th...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12039.x