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. 1987 Nov-Dec;69(11-12):1175-81.
doi: 10.1016/0300-9084(87)90144-1.

Yeast phenylalanyl-tRNA synthetase: evidence for the formation of ADP by phosphorolysis of enzyme-bound aminoacyladenylate

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Yeast phenylalanyl-tRNA synthetase: evidence for the formation of ADP by phosphorolysis of enzyme-bound aminoacyladenylate

G Guédon et al. Biochimie. 1987 Nov-Dec.

Abstract

ADP and Ap3A are synthesized by the yeast phenylalanyl-tRNA synthetase, according to reaction pathways similar to the pyrophosphorolysis of the intermediate aminoacyladenylate or to the one leading to Ap4A synthesis. The enzyme-bound phenylalanyladenylate reacts with inorganic phosphate or ADP to yield, respectively, ADP or Ap3A. The rate of synthesis is strongly stimulated by Zn2+. This new phosphorolysis activity accounts for the complex pattern of bisnucleoside polyphosphate syntheses starting from ATP.

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