RRC ID 6997
著者 Arai T, Kino K.
タイトル New L-amino acid ligases catalyzing oligopeptide synthesis from various microorganisms.
ジャーナル Biosci Biotechnol Biochem
Abstract 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.
巻・号 74(8)
ページ 1572-7
公開日 2010-1-1
DOI 10.1271/bbb.100148
PII JST.JSTAGE/bbb/100148
PMID 20699590
MeSH Amino Acids / metabolism* Bacteria / metabolism* Biocatalysis* Computational Biology* Dipeptides / metabolism Ligases / chemistry Ligases / metabolism* Molecular Weight Oligopeptides / biosynthesis*
IF 1.516
引用数 12
WOS 分野 FOOD SCIENCE & TECHNOLOGY CHEMISTRY, APPLIED BIOTECHNOLOGY & APPLIED MICROBIOLOGY BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
一般微生物 JCM 1275