58607-69-5Relevant articles and documents
Search for fibrous aggregates potentially useful in regenerative medicine formed under physiological conditions by self-assembling short peptides containing two identical aromatic amino acid residues
Fraczyk, Justyna,Lipinski, Wojciech,Chaberska, Agata,Wasko, Joanna,Rozniakowski, Kamil,Kaminski, Zbigniew J.,Bogun, Maciej,Draczynski, Zbigniew,Menaszek, Elzbieta,Stodolak-Zych, Ewa,Kaminska, Marta,Kolesinska, Beata
supporting information, (2018/03/21)
This study investigates the propensity of short peptides to self-organize and the influence of aggregates on cell cultures. The dipeptides were derived from both enantiomers of identical aromatic amino acids and tripeptides were prepared from two identica
Aminolytic reaction catalyzed by d-stereospecific amidohydrolases from Streptomyces spp
Arima, Jiro,Ito, Hitomi,Hatanaka, Tadashi,Mori, Nobuhiro
experimental part, p. 1460 - 1469 (2012/01/12)
From investigation of 2000 soil isolates, we identified two serine-type amidohydrolases that can hydrolyze d-aminoacyl derivatives from the culture supernatant of Streptomyces species 82F2 and 83D12. The enzymes, redesignated as 82F2-DAP and 83D12-DAP, were purified for homogeneity and characterized. Each enzyme had molecular mass of approximately 40 kDa, and each showed moderate stability with respect to temperature and pH. Among hydrolytic activities toward d-aminoacyl-pNAs, the enzymes showed strict specificity toward d-Phe-pNA, but showed broad specificity toward d-aminoacyl esters. The specific activity for d-Phe-pNA hydrolysis of 82F2-DAP was ten-fold higher than that of 83D12-DAP. As a second function, each enzyme showed peptide bond formation activity by its function of aminolysis reaction. Based on results of d-Phe-d-Phe synthesis under various conditions, we propose a reaction mechanism for d-Phe-d-Phe production. Furthermore, the enzymes exhibited peptide elongation activity, producing oligo homopeptide in a one-pot reaction. We cloned the genes encoding each enzyme, which revealed that the primary structure of each enzyme showed 30-60% identity with those of peptidases belonging to the clan SE, S12 peptidase family categorized as serine peptidase with d-stereospecificity.