Kinetic studies of adenine phosphoribosyltransferase.
作者： Makoto Hori , J. Frank Henderson
DOI: 10.1016/S0021-9258(18)96478-1
关键词:
摘要: Abstract The mechanism of reaction adenine phosphoribosyl-transferase from Ehrlich ascites tumor cells was investigated kinetically by initial velocity and product inhibition studies. data are consistent with a in which 5-phosphoribosylpyrophosphate reacts the enzyme to form an intermediate, presumably enzyme-ribose 5-phosphate complex, then adenylate. Noncompetitive inorganic pyrophosphate respect suggests that former binds tightly enzyme-adenylate complex. Both PP-ribose-P PPi participate their magnesium complexes.
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