Pyridoxamine phosphate transaminase
نویسندگان
چکیده
منابع مشابه
Reaction of Pyridoxamine - Pyruvate Transaminase Sulfhydryl Reagents
Wherever the point has been examined (e.g. References l-6), pyridoxal phosphate enzymes have been found to require free sulfhydryl groups for activity. The functional role played by these groups, however, has not been clear. In glutamate-oxaloacetate transaminase, which has been studied most extensively, no spectrophotometric or enzymatic evidence for their participation in coenzyme binding was...
متن کاملInteraction of Pyridoxamine-pyruvate Transaminase with Carbonyl Derivatives of Pyridoxal.
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 کاملThe pyridoxal-binding site in pyridoxamine-pyruvate transaminase.
The enzyme-substrate complex formed between pyridoxamine-pyruvate transaminase (EC 2.6.1.30) and pyridoxal was reduced with NaBH4. After carboxymethylation and tryptic digestion, pyridoxyl-lysine-containing peptides were isolated by a combination of Sephadex and Dowex 50 chromatography. Analysis of these peptides shows the structure around the pyridoxal-binding lysine residues to be Ala-Asp-Ile...
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: Biochemical Journal
سال: 1957
ISSN: 0306-3283
DOI: 10.1042/bj0660520