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

Guédon, G.; Ebel, J.P.; Remy, P.

Biochimie 69(11-12): 1175-1181

1987


ISSN/ISBN: 0300-9084
PMID: 3129022
DOI: 10.1016/0300-9084(87)90144-1
Accession: 041992534

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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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