Pig Heart Glutamic Aspartic Transaminase Mechanism of Transamination.
نویسندگان
چکیده
24 Rumberg, B., A. Muller, and H. T. Witt, Nature, 194, 854 (1962). 25 Duysens, L. M. N., and J. Amesz, Biochim. et Biophys. Acta, 64, 261 (1962). 26 Crane, F. L., in CIBA Foundation Symposium on Quinones in Electron Transport (London, 1960), ed. C. E. W. Wolstenholme and C. K. O'Connor (London: J. & A. Churchill, Ltd., 1961), p. 36. 27 Clayton, R. K., Biochem. Biophys. Res. Comm., 9, 49 (1962). 28 Chance, B., and G. Hollunger, Nature, 185, 666 (1960). 29 Low, H., and I. Vallin, Biochim. et Biophys. Acta, 69, 361 (1963).
منابع مشابه
Glutamic Aspartic Transaminase
Aspartate and glutamate react instantaneously with the pyridoxal form of the pig heart glutamic aspartic transaminase (1) to yield the corresponding keto acid, converting the enzymebound pyridoxal phosphate to bound pyridoxamine phosphate (2). Other amino acids such as methionine sulfoxide, methionine sulfone, and alanine react much more slowly with the enzyme, but the reaction itself appears t...
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Pig heart “soluble” glutamic-aspartic transaminase (L-aspartate : 2-oxoglutarate aminotransferase, EC 2.6.1.1) will catalyze the exchange of an amino group between glutamate and ketoglutarate without the participation of any other amino acid or keto acid (1). This “exchange transamination” also occurs between aspartate and oxaloacetate. The rates of these reactions are comparable to the physiol...
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عنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 49 5 شماره
صفحات -
تاریخ انتشار 1963