Improved substrate specificity of water-soluble pyrroloquinoline quinone glucose dehydrogenase by a peptide ligand.

Yoshida, Hiromi; Yagi, Yukiko; Ikebukuro, Kazunori; Sode, Koji

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.

PQQ (Biochemistry); DEHYDROGENASES; GLUCOSE; PEPTIDES; LIGANDS (Biochemistry); DISACCHARIDES

Biotechnology Letters, 2003, Vol 25, Issue 4, p301

0141-5492

Academic Journal

10.1023/A:1022345200666