Development of a method for enzymatic protein modification with polyamine chains

2019 Fiscal Year Final Research Report

• Project/Area Number: 18K19180
• Research Category: Grant-in-Aid for Challenging Research (Exploratory)
• Allocation Type: Multi-year Fund
• Review Section: Medium-sized Section 38:Agricultural chemistry and related fields
• Research Institution: Hiroshima University
• Principal Investigator: Ikeda Takeshi 広島大学, 統合生命科学研究科(先), 助教 (10505754)
• Project Period (FY): 2018-06-29 – 2020-03-31
• Keywords: 酵素 / ポリアミン / タンパク質修飾

Outline of Final Research Achievements

Our previous results suggested that an aminopropyltransferase with low substrate specificity is present in some bacteria. We hypothesized that this enzyme could be used for protein modification by transferring aminopropyl groups to the side chain of lysine residues, whose chemical structure is similar to that of polyamines. In this study, the enzyme of interest was identified and found to show low substrate specificity as expected. However, unfortunately we could not confirm whether this enzyme transfers aminopropyl groups to a lysine side chain, because the detection of target products was interfered by the presence of reaction byproducts.

Free Research Field

生物工学

Academic Significance and Societal Importance of the Research Achievements

以前からその存在が予想されていた基質特異性の低いアミノプロピル基転移酵素を同定し、その基質特異性を評価することに成功した。本酵素が、タンパク質をポリアミンで修飾する技術に利用できるかについては明らかにできなかったため、さらなる研究が必要である。タンパク質をポリアミンで修飾できれば、シリカへの親和性や細胞膜透過効果などの有用な性質をタンパク質に付与できると期待される。