Substrate specificities of artificial flavo-enzymes

Autor: Hideo Akisada, Norikazu Nishino, Y. Kakimoto, Kin-ya Tomizaki
Rok vydání: 2006
Předmět:
Zdroj: Peptide Science — Present and Future ISBN: 0792352718
DOI: 10.1007/0-306-46864-6_22
Popis: Previously, we have synthesized a 53-peptide containing Cys(Fla) residues at the hydrophobic side of the four α -helix bundle structure (Figure 1). The 53-peptide exhibi ted the catalyt ic act ivi ty toward the oxidat ion of 1-benzyl-1,4-dihydronicotinamide (Bzl-NAH) in the presence of sodium dodecylsulfate (SDS) [1]. Instead of the addition of a surfactant, we modified the substrate with various alkyl chains to evaluate the specificity. In addition, in order to compare the positioning of Cys(Fla) on the amphiphilic α-helix, we synthesized the related 53-peptides with different sequences for Cys (Figure 1A).
Databáze: OpenAIRE