Metal binding to pyridoxal derivatives. An NMR study of the interaction of Eu(III) with pyridoxal phosphate and pyridoxamine phosphate
نویسندگان
چکیده
منابع مشابه
Binding of Pyridoxal 5'-Phosphate
1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo(a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the...
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on pyridoxine or pyridoxamine as a sole source of carbon and nitrogen (1, 2). This transaminase contains no pyridoxal phosphate, and hence provides a simpler system for mechanistic studies than do the more complex, pyridoxal phosphate-containing transaminases. The enzyme binds pyridoxamine and pyridoxal with almost equal avidity; the latter is bound in part by an azomethine Iinkage to the e-ami...
متن کاملBinding of pyridoxal 5-phosphate to cystathionase.
The binding of pyridoxal 5-phosphate to the apoprotein of the enzyme cystathionase from rat liver was investigated by two independent methods, absorption and fluorescence spectroscopy. The increase in absorbance at 525 nm associated with Schiff’s base formation was used to investigate the binding of pyridoxal-5-P at a protein concentration of 1 X 10e5 M. A model based on two classes of independ...
متن کاملEnzymatic oxidation of pyridoxamine phosphate to pyridoxal phosphate in rabbit liver.
In the course of testing the possible coenzymic function of the phosphorylated vitamin B, derivatives on the synthesis of glucosamine 6-phosphate by a rat liver preparation, the appearance of a yellow color similar to that of pyridoxal 5-phosphate was observed in the samples containing pyridoxamine 5-phosphate. Further investigation has revealed the presence of a soluble enzyme system in extrac...
متن کاملPyridoxamine phosphate-oxidase and pyridoxal phosphate-phosphatase activities in Escherichia coli.
acetone), than found in earlier investigations. Mayer (1930) used a concentration of 66% for his determinations, but this is definitely inhibitory, though lese so for insoluble preparations than for soluble. The enzyme is remarkably stable before it becomes soluble and the activity of soluble preparations is retained well in the cold. The optimum temperature for enzyme action is much lower than...
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ژورنال
عنوان ژورنال: Journal of Biosciences
سال: 1979
ISSN: 0250-5991,0973-7138
DOI: 10.1007/bf02702885