The Interaction of Pyridoxamine 5-Phosphate with Aspartate Aminotransferase
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منابع مشابه
The 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 کاملMechanism of binding of pyridoxamine 5-phosphate to the apoenzyme aspartate aminotransferase. Fluorescence studies.
The combination of pyridoxamine 5-phosphate with the apoprotein of the enzyme aspartate aminotransferase has been followed by measuring the quenching of protein fluorescence associated with complex formation. The reaction takes place in two steps; an initial rapid decrease in protein fluorescence is followed by a slow quenching process which parallels the recovery of catalytic activity. Similar...
متن کاملTransfer of pyridoxal 5'-phosphate from albumin-pyridoxal 5'-phosphate complex to apo-aspartate aminotransferase.
Pyridoxal 5•L-phosphate (PLP) is known to combine with bovine serum albumin to form a(1:1) complex which scarcely dissociates, even when subjected to intensive dialysis. When this complex was incubated with apo-aspartate aminotransferase (apoGOT) for an appropriate time and the preincubated mixture then submitted to the usual GOT assay, the appearance of GOT activity was obviously confirmed, in...
متن کاملInfluence of pyridoxal-5'-phosphate on the determination of the alanine aminotransferase and aspartate aminotransferase of commercial test sera.
The influence of pyridoxal-5'-phosphate on the activities of alanine aminotransferase and aspartate aminotransferase from commercial test sera was investigated. Enhancement of the activity of alanine aminotransferase by the coenzyme is about 20% when 0.1 mmol/1 of pyridoxal-S'-phosphate is added to the reaction medium. This concentration seems sufficient for full saturation of the apoenzyme. Fo...
متن کاملCrystal structures of aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate: internal aldimine and stable L-aspartate external aldimine.
The 1.8 Å resolution crystal structures of Escherichia coli aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate (deazaPLP; 2-formyl-3-hydroxy-4-methylbenzyl phosphate) in the internal aldimine and L-aspartate external aldimine forms are reported. The L-aspartate·deazaPLP external aldimine is extraordinarily stable (half-life of >20 days), allowing crystals of this interm...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)78193-9