Synthesis of (di)adenosine polyphosphates by non-ribosomal peptide synthetases (NRPS)

被引:23
作者
Dieckmann, R
Pavela-Vrancic, M
von Döhren, H
机构
[1] Tech Univ Berlin, Max Volmer Inst Biophys Chem & Biochem, D-10587 Berlin, Germany
[2] Univ Split, Fac Nat Sci Math & Educ, Dept Chem, Split 21000, Croatia
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2001年 / 1546卷 / 01期
关键词
peptide synthetase; tyrocidine synthetase 1; (di)nucleoside polyphosphate; (di)adenosine tetraphosphate; Bacillus brevis;
D O I
10.1016/S0167-4838(01)00146-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In response to nutritional stress conditions, Bacillus brevis produces the cyclodecapeptide antibiotic tyrocidine via tyrocidine synthetase, a multifunctional non-ribosomal peptide synthetase. The ape-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. (C) 2001 Published by Elsevier Science B.V.
引用
收藏
页码:234 / 241
页数:8
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