Independent Modification of the Binding Sites for Adenosine Diphosphate and L-Threonine in Threonine Dehydratase
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چکیده
منابع مشابه
Purification and regulatory properties of the adenosine diphosphate-activated threonine dehydratase.
The ADP-activated threonine dehydratase of Closfridium fefanomorphum has been purified approximately llOO-fold in 20% yield and crystallized. Such preparations are homogeneous when examined by sedimentation, electrophoretic, and immunological techniques. The pure enzyme displays an absorption maximum at 415 rnp in neutral solutions, which is consistent with a Schiff base linkage between pyridox...
متن کاملOn the mechanism of activation of L-threonine deaminase from Clostridium tetanomorphum by adenosine diphosphate.
In order to clarify the mechanism of activation of L-threonine deaminase by adenosine diphosphate, the enzyme was purified about 700.fold from sonic extracts of Closlridium tetanomorphum, and kinetic and ADP-binding studies were carried out. Plots of reaction rates against L-threonine concentrations gave a sigmoid curve in the absence of ADP, whereas a hyperbolic curve was obtained in the prese...
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A timeand concentration-dependent irreversible inactivation of the Escherichia coli biodegradative threonine dehydratase by glyoxylate is accompanied by enzyme aggregation, apparent covalent binding of 4 mol of glyoxylate/mol of aggregated species, and a displacement of the absorption maximum of the enzyme-bound pyridoxal phosphate from 413 to 388 nm (Park, L. S., and Datta, P. (1979) J Biol. C...
متن کاملMolecular Evolution of Threonine Dehydratase in Bacteria
Threonine dehydratase converts L-threonine to 2-ketobutyrate. Several threonine dehydratases exist in bacteria, but their origins and evolutionary pathway are unknown. Here we analyzed all the available threonine dehydratases in bacteria and proposed an evolutionary pathway leading to the genes encoding three different threonine dehydratases CTD, BTD1 and BTD2. The ancestral threonine dehydrata...
متن کاملIsolation and Properties of a Homogeneous Preparation of Cystathionine Synthetase-l-serine and L-threonine Dehydratase.
Selim and Greenberg (1, 2) achieved a considerable degree of purification of L-serine dehydratase (L-serine hydro-lyase (deaminating), EC 4.2.1.13) from rat liver and demonstrated that this protein preparation contained the cystathionine-synthesizing activity of the liver (L-serine hydro-lyase (adding L-homocysteine), EC 4.2.1.21). These workers (2) also observed activity of their enzyme prepar...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)94275-4