Intracellular localization of pyridoxamine-5-phosphate oxidase in rabbit liver
نویسندگان
چکیده
منابع مشابه
Enzymatic 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 کاملKinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12.
We report the purification and enzymological characterization of Escherichia coli K-12 pyridoxine (pyridoxamine) 5'-phosphate (PNP/PMP) oxidase, which is a key committed enzyme in the biosynthesis of the essential coenzyme pyridoxal 5'-phosphate (PLP). The enzyme encoded by pdxH was overexpressed and purified to electrophoretic homogeneity by four steps of column chromatography. The purified Pd...
متن کاملPyridoxamine-5'-phosphate oxidase exhibits no specificity in prochiral hydrogen abstraction from substrate.
The stereochemistry for hydrogen removal from pyridoxamine 5'-phosphate with liver pyridoxine (pyridoxamine)-5'-phosphate oxidase was examined to determine whether or not there are significant steric constraints at the substrate region of the active site of the oxidase. For this, pyridoxal 5'-phosphate was reduced with tritium-labeled sodium borohydride in ammoniacal solution to yield racemical...
متن کاملThe interaction of pyridoxamine 5-phosphate with aspartate aminotransferase.
The binding of pyridoxamine 5-phosphate to the enzyme aspartate aminotransferase from pig heart was investigated by fluorescence spectroscopy. The substantial decrease in fluorescence intensity at 390 rnp that follows the interaction of pyridoxamine 5-phosphate with the apoenzyme was used to determine the alhnity constant. The effect of pH on the stability of the apoenzyme-pyridoxamine 5-phosph...
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: FEBS Letters
سال: 1974
ISSN: 0014-5793
DOI: 10.1016/0014-5793(74)80941-5