Synthesis of (di)adenosine polyphosphates by non-ribosomal peptide synthetases (NRPS).
In response to nutritional stress conditions, Bacillus brevis produces the cyclodecapeptide antibiotic tyrocidine via tyrocidine synthetase, a multifunctional non-ribosomal peptide synthetase. The apo-form of tyrocidine synthetase 1 forms adenosine (5')tetraphospho(5')adenosine, when incubated with MgATP(2-), amino acid and inorganic pyrophosphatase. The synthesis is an intrinsic property of the adenylation domain, is strictly dependent upon the amino acid, and proceeds from a reverse reaction of adenylate formation involving a second ATP molecule. In the presence of tri- or tetrapolyphosphate preferential synthesis of adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate occurs, respectively. A potential involvement of adenosine (5')-n-phospho(5')adenosine in the regulation of the biosynthetic process has been suggested.
Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Franklinstrasse 20, 10587 Berlin, Germany.
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Dieckmann
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Pavela-Vrancic
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von Döhren
D000255:Adenosine Triphosphate / Q000378:metabolism; D015226:Dinucleoside Phosphates / Q000096:biosynthesis / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D010453:Peptide Synthases / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids; D011755:Pyrophosphatases; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D015226:Dinucleoside Phosphates; C020733:diadenosine tetraphosphate; D000255:Adenosine Triphosphate; D011755:Pyrophosphatases; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase; C035180:tyrocidine synthetase