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Glu742 substitution to Lys enhances the EDTA tolerance ofEscherichia coli PQQ glucose dehydrogenase |
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| Authors: | Koji Sode Hiroyuki Sano |
| Institution: | (1) Department of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184 Koganei, Tokyo, Japan |
| Abstract: | Summary Based on homology analysis of the PQQ (pyrroloquinoline quinone) glucose dehydrogenase (PQQGDH) gene fromEscherichia coli andAcinetobacter calcoaceticus, Glu742 was substituted to Lys by site directed mutagenesis of theE. coli PQQGDH gene (gcd). The mutant enzyme, E742K showed higher tolerance towards EDTA inactivation than wild type PQQGDH. This is the first mutagenesis study of putative a PQQ binding site in PQQ enzyme. |
| Keywords: | Pyrroloquinoline quinone (PQQ) Quinoprotein glucose dehydrogenase (GDH) putative PQQ binding site site directed mutagenesis Escherichia coli Acinetobacter calcoaceticus |
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