Autor: Koji Sode, Hiromi Yoshida, Kazunori Ikebukuro, Yukiko Yagi
Rok vydání: 2003
Předmět:
Zdroj: Biotechnology Letters. 25:301-305
ISSN: 0141-5492
DOI: 10.1023/a:1022345200666
Popis: A new approach in altering the substrate specificity of enzyme is proposed using glucose dehydrogenase, with pyrroroquinoine quinone (PQQGDH) as co-factor, as the model. This approach is based on the selection of random peptide phage displayed library. Using an M13 phage-display random peptide library, we have selected peptide ligands. Among the peptide ligands, a 7-mer peptide, composed of Thr-Thr-Ala-Thr-Glu-Tyr-Ser, caused PQQGDH substrate specificity to decrease significantly toward disaccharides, such as maltose and lactose, while a smaller effect was observed toward glucose. Consequently, this peptide narrowed the substrate specificity of PQQGDH, without a significant loss of the enzyme activity.
Databáze: OpenAIRE