Firefly luciferase synthesizes P1,P4-bis(5'-adenosyl)tetraphosphate (Ap4A) and other dinucleoside polyphosphates.
The synthesis of P1,P4-bis(5'-adenosyl)tetraphosphate (Ap4A) has been considered, for a long time, to be catalyzed mainly by some aminoacyl-tRNA synthetases [Brevet et al. (1989) Proc. Natl. Acad. Sci. USA 86, 8275-8279]. Recently, yeast Ap4A phosphorylase, acting in reverse (Guranowski et al. (1988) Biochemistry 27, 2959-2964), was shown to synthesize Ap4A, too. In the case of the synthetases, the intermediate complex E-aminoacyl-AMP may serve as donor of AMP to ATP, yielding Ap4A. Here we demonstrate that firefly luciferase (EC 1.13.12.7) which forms the E-luciferin-AMP intermediate also synthesizes Ap4A as well as other dinucleoside polyphosphates. We suggest moreover that: other enzymes (mainly synthetases and some transferases), which catalyze the transfer of a nucleotidyl moiety, via nucleotidyl-containing intermediates and releasing PPi may produce dinucleoside polyphosphates.
Guranowski
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Departamento de Bioquímica, CSIC, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.
Sillero
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MA
Sillero
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A
D015226:Dinucleoside Phosphates / Q000138:chemical synthesis*; D011756:Diphosphates / Q000378:metabolism; D008156:Luciferases / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism
D015226:Dinucleoside Phosphates; D011756:Diphosphates; C020733:diadenosine tetraphosphate; D008156:Luciferases; D011755:Pyrophosphatases