New L-Amino Acid Ligases Catalyzing Oligopeptide Synthesis from Various Microorganisms
New L-Amino Acid Ligases Catalyzing Oligopeptide Synthesis from Various Microorganisms
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DOI：
10.1271/bbb.100148
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发表时间：
2010-08-01
影响因子：
1.6
通讯作者：
Kino, Kuniki
中科院分区：
文献类型：
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作者：
Arai, Toshinobu;Kino, Kuniki
L-氨基酸连接酶以ATP依赖的方式从未保护的L-氨基酸合成各种肽。已知的L-氨基酸连接酶仅催化二肽合成，但最近我们发现枯草芽孢杆菌NBRC 3134的RizB催化寡肽合成。在本研究中，我们寻找新成员的L-氨基酸连接酶组催化寡肽合成。通过计算机分析选择了几种具有ATP-抓取基序的假设蛋白质。测定这些重组蛋白的L-氨基酸连接酶活性。我们获得了五个L-氨基酸连接酶显示寡肽合成活动。这些蛋白质在氨基酸序列上的相似性较低，但通常使用支链氨基酸，如RizB，作为底物。此外，肺炎链球菌的spr 0969蛋白合成的肽比RizB合成的肽长，双歧杆菌的BAD_1200蛋白对芳香族氨基酸的活性比对支链氨基酸的活性高。我们还研究了它们的一些特征。
L-Amino acid ligase synthesizes various peptides from unprotected L-amino acids in an ATP-dependent manner. Known L-amino acid ligases catalyze only dipeptide synthesis, but recently we found that RizB of Bacillus subtilis NBRC 3134 catalyzes oligopeptide synthesis. In the present study, we searched for new members of the L-amino acid ligase group that catalyze oligopeptide synthesis. Several hypothetical proteins possessing the ATP-grasp motif were selected by in silico analysis. These recombinant proteins were assayed for L-amino acid ligase activity. We obtained five L-amino acid ligases showing oligopeptide synthesis activities. These proteins showed low similarity in amino acid sequence, but commonly used branched-chain amino acids, such as RizB, as substrates. Furthermore, the spr0969 protein of Streptococcus pneumoniae synthesized longer peptides than those synthesized by RizB, and the BAD_1200 protein of Bifidobacterium adolescentis showed higher activity toward aromatic amino acids than toward branched-chain ones. We also examined some of their characteristics.