論文 - 詳細
| RRC ID | 5727 |
|---|---|
| 著者 | Kino K, Nakazawa Y, Yagasaki M. |
| タイトル | Dipeptide synthesis by L-amino acid ligase from Ralstonia solanacearum. |
| ジャーナル | Biochem Biophys Res Commun |
| Abstract |
Despite its utility, dipeptides have not been widely used due to the absence of an efficient manufacturing method. Recently, a novel method for effective production of dipeptides using l-amino acid alpha-ligase (Lal) is presented. Lal, which is only identified in Bacillus subtilis, catalyzes dipeptide synthesis from unprotected amino acids in an ATP-dependent manner. However, not all the dipeptide can be synthesized by Lal from B. subtilis (BsLal) due to its substrate specificity. Here, we attempted to find a novel Lal exhibiting different substrate specificity from BsLal. By in silico screening based on the amino acid sequence of BsLal, RSp1486a an unknown protein from Ralstonia solanacearum was found to show the Lal activity. RSp1486a exhibited different substrate specificity from BsLal, and preferably synthesized hetero-dipeptides where more bulky amino acid was placed at N terminus and less bulky amino acid was placed at C terminus in opposition to those synthesized by BsLal. |
| 巻・号 | 371(3) |
| ページ | 536-40 |
| 公開日 | 2008-7-4 |
| DOI | 10.1016/j.bbrc.2008.04.105 |
| PII | S0006-291X(08)00798-5 |
| PMID | 18445480 |
| MeSH | Dipeptides / biosynthesis* Dipeptides / chemistry Escherichia coli / genetics Peptide Synthases / chemistry* Peptide Synthases / genetics Peptide Synthases / isolation & purification Plant Proteins / chemistry* Plant Proteins / genetics Plant Proteins / isolation & purification Protein Conformation Ralstonia solanacearum / enzymology* Ralstonia solanacearum / genetics Substrate Specificity |
| IF | 2.985 |
| 引用数 | 28 |
| WOS 分野 | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 5 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 一般微生物 | JCM10489 |