| ENGINEERING | ORGANISM | UNIPROT ACCESSION NO. | COMMENTARY | LITERATURE |
| A71P/N454S | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.95, substrate maltose 0.75 | 671548 |
| A98G/K126R/L445I/N454S | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78 | 671548 |
| D167A | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167C | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167E | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, slightly reduced activity compared to the wild-type enzyme | 654947 |
| D167E/N452T | Acinetobacter calcoaceticus | - | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | 654947 |
| D167G | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167H | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167K | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167N | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167Q | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167R | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167S | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167V | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167W | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D167Y | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, reduced activity compared to the wild-type enzyme | 654947 |
| D276E | Acinetobacter calcoaceticus | - | drastic decrease in EDTA tolerance | 639216 |
| E277A | Acinetobacter calcoaceticus | - | decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| E277D | Acinetobacter calcoaceticus | - | decreased Km value for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| E277G | Acinetobacter calcoaceticus | - | drastic decrease in EDTA tolerance | 639216 |
| E277H | Acinetobacter calcoaceticus | - | decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| E277K | Acinetobacter calcoaceticus | - | decreased Km value for glucose and altered substrate specificity, significantly increased catalytic efficiency compared with the wild-type enzyme | 639216 |
| E277N | Acinetobacter calcoaceticus | - | decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| E277Q | Acinetobacter calcoaceticus | - | decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| E277V | Acinetobacter calcoaceticus | - | decreased Km values for glucose and altered substrate specificity, thermal stability is less than 20% of that of the wild-type enzyme | 639216 |
| G100R | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.35, substrate maltose 0.26 | 671548 |
| G100W/G320E/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.55, substrate maltose 0.20 | 671548 |
| G320D/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.51, substrate maltose 0.16; mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.24 | 671548 |
| G320E | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.70 | 671548 |
| G320E/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.69, substrate maltose 0.25 | 671548 |
| G320F/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.48, substrate maltose 0.17 | 671548 |
| G320Y/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.49, substrate maltose 0.16 | 671548 |
| H168C | Acinetobacter calcoaceticus | - | site-directed mutagenesis, catalytic residue mutation, highly reduced activity compared to the wild-type enzyme | 654947 |
| H168Q | Acinetobacter calcoaceticus | - | site-directed mutagenesis, catalytic residue mutation, nearly inactive mutant | 654947 |
| H168Q | Acinetobacter calcoaceticus | - | site-directed mutagenesis, inactive mutant, a heterodimeric chimeric enzyme consisiting of 1 wild-type subunit and 1 mutant subunit shows decreased activity and a substrate specificity similar to the wild-type enzyme | 655929 |
| K166E | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| K166G | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| K166I | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| K3E/E278G/G392C | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.92, substrate maltose 0.53 | 671548 |
| L194F/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.39, substrate maltose 0.075 | 671548 |
| L194F/G320E/M367P | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.14 | 671548 |
| L194F/G320E/M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.36, substrate maltose 0.051 | 671548 |
| L194F/G320F | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.38, substrate maltose 0.060 | 671548 |
| L194Q | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.22, substrate maltose 0.15 | 671548 |
| N275E | Acinetobacter calcoaceticus | - | drastic decrease in EDTA tolerance | 639216 |
| N340F/Y418F | Acinetobacter calcoaceticus | - | site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme | 655127 |
| N340F/Y418I | Acinetobacter calcoaceticus | - | site-directed mutagenesis, mutation of residues at the dimer interface, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme | 655127 |
| N452T | Acinetobacter calcoaceticus | - | site-directed mutagenesis, reduced activity compared to the wild-type enzyme | 654947 |
| N454S | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.87, substrate maltose 0.69 | 671548 |
| Q169E | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| Q169K | Acinetobacter calcoaceticus | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| Q193H | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.41, substrate maltose 0.23 | 671548 |
| Q193S/G320E | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.56, substrate maltose 0.19 | 671548 |
| Q209R/N240R/T389R | Acinetobacter calcoaceticus | - | site-directed mutagenesis, increased thermal stability compared to the wild-type enzyme | 655097 |
| S231C | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| S231D | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| S231H | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| S231K | Acinetobacter calcoaceticus | - | more than 8fold increase in its half-life during the thermal inactivation at 55 C compared with the wild-type enzyme, retains catalytic activity similar to the wild-type enzyme | 639218 |
| S231L | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| S231M | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| S231N | Acinetobacter calcoaceticus | - | increase in thermal stability | 639218 |
| T348G | Acinetobacter calcoaceticus | - | mutant crystallized by microseeding, data set is collected at 2.36 A resolution | 671165 |
| T348G/N428P | Acinetobacter calcoaceticus | - | mutant crystallized by microseeding, data set is collected at 2.15 A resolution | 671165 |
| T416V/T417V | Acinetobacter calcoaceticus | - | site-directed mutagenesis, mutation of resides of the hydrophobic region, 2fold increased thermal stability at 55°C and unaltered catalytic efficiency compared to the wild-type enzyme | 655127 |
| V157I/M367V/T463S | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 1.00, substrate maltose 0.78 | 671548 |
| V91A/W372R | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.44, substrate maltose 0.22 | 671548 |
| Y171G/E245D/M341V/T348G/N428P | Acinetobacter calcoaceticus | - | mutant crystallized by microseeding, data set is collected at 2.20 A resolution | 671165 |
| Y248F/N342D/A376T/A418V | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.74, substrate maltose 0.43 | 671548 |
| Y302H | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.47, substrate maltose 0.35 | 671548 |
| D204A | Escherichia coli | - | no GDH activity | 712800 |
| D354N | Escherichia coli | P15877 | site-directed mutagenesis, 9% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | 654865 |
| D354N | Escherichia coli | - | mutant retains a conformation almost unaltered compared to the wild type mGDH and strongly reduced activity | 687745 |
| D354N/N355D | Escherichia coli | P15877 | site-directed mutagenesis, 10% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | 654865 |
| D448N | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| D456N | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| D457N | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| D466E | Escherichia coli | - | very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme | 639208 |
| D466E | Escherichia coli | - | mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme | 687745 |
| D466N | Escherichia coli | - | very low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone | 639208 |
| D466N | Escherichia coli | - | mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme | 687745 |
| D730A | Escherichia coli | - | low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate | 639210 |
| D730N | Escherichia coli | - | low glucose oxidase activity without influence on the affinity for pyrroloquinoline quinone, Mg2+ or substrate | 639210 |
| D730R | Escherichia coli | - | reduced affnity for pyrroloquinoline quinone | 639210 |
| E217A | Escherichia coli | - | no GDH activity | 712800 |
| E217L | Escherichia coli | - | no GDH activity | 712800 |
| E217Q | Escherichia coli | - | the mutant retains its function similar to that of wild type GDH | 712800 |
| E591K | Escherichia coli | - | no GDH activity | 712800 |
| E591L | Escherichia coli | - | no GDH activity | 712800 |
| E591Q | Escherichia coli | - | no GDH activity | 712800 |
| E742G/P757L | Escherichia coli | - | slightly higher Km value for Mg2+ | 639210 |
| G689D | Escherichia coli | - | significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+ | 639210 |
| G776A | Escherichia coli | - | the mutant retains its function similar to that of wild type GDH | 712800 |
| G776D | Escherichia coli | - | no GDH activity | 712800 |
| G776K | Escherichia coli | - | no GDH activity | 712800 |
| G776L | Escherichia coli | - | no GDH activity | 712800 |
| H262A | Escherichia coli | - | reduced affinity both for glucose, 11fold, and pyrroloquinoline quinone, 8fold, without significant effect on glucose oxidase activity | 639208 |
| H262Y | Escherichia coli | - | greatly diminished catalytic efficiency for all substrates, rate of electron transfer to oxygen is unaffected, 230fold increased Km value for glucose | 639213 |
| H775A | Escherichia coli | - | pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone | 639210 |
| H775R | Escherichia coli | - | pronounced reduction of affinity for the prosthetic group pyrroloquinoline quinone, 230fold higher Km than wild-type enzyme | 639210 |
| K493A | Escherichia coli | - | very low glucose oxidase activity, without influence on the affinity for pyrroloquinoline quinone, very low activity with ubiquinone Q2 compared with the wild-type enzyme, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type | 639208 |
| K493A | Escherichia coli | - | mutant shows no significant difference in molecular structure from that of the wild type mGDH but has remarkably reduced content of bound ubiquinone and less than 0.04% activity compared to the wild type enzyme | 687745 |
| K493R | Escherichia coli | - | pronounced reduction of affinity for pyrroloquinoline quinone, very low activity of both phenazine methosulfate reductase and glucose oxidase in the membrane fractions compared with the wild type | 639208 |
| K493R | Escherichia coli | - | mutant retains a conformation almost unaltered compared to the wild type mGDH, the rate of ubiquinone to pyrroloquinoline electron transfer is about 4fold slower than that of the wild type enzyme, shows less than 0.04% activity compared to the wild type enzyme | 687745 |
| L712R | Escherichia coli | - | no GDH activity | 712800 |
| N355D | Escherichia coli | P15877 | site-directed mutagenesis, 25% of wild-type activity, mutant enzyme can be reconstituted with PQQ and Ca2+, Sr2+, or Ba2+, but not with Mg2+, which functions as a competitive inhibitor, in contrary to the wild-type enzyme | 654865 |
| N452D | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N452H | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N452I | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N452K | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N452T | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows narrowed substrate specificity, but unaltered catalytic efficiency, thermal stability, and EDTA tolerance compared to the wild-type isozyme PQQGDH-B | 654398 |
| N462D | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N462H | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N462K | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| N462Y | Escherichia coli | - | site-directed mutagenesis, mutation in the active site loop 6BC region, mutant shows altered substrate specificity, but unaltered catalytic efficiency with D-glucose, compared to the wild-type isozyme PQQGDH-B | 654398 |
| R201A | Escherichia coli | - | no GDH activity | 712800 |
| R266E | Escherichia coli | - | no GDH activity | 712800 |
| R266Q | Escherichia coli | - | no GDH activity | 712800 |
| S145C | Escherichia coli | - | site-directed mutagenesis, introduction of a Cys residue in each monomer of the enzyme leads to formation of an intersubunit disulfide bridge at the dimer interface resulting in 30fold increased thermal stability at 55°C compared to the wild-type enzyme | 656767 |
| S357L | Escherichia coli | - | significantly increased Km for pyrroloquinoline quinone, slightly higher Km value for Mg2+ | 639210 |
| W404A | Escherichia coli | - | pronounced reduction of affinity for pyrroloquinoline quinone, very low glucose oxidase activity and phenazine methosulfate reductase activity compared with wild-type enzyme | 639208 |
| W404F | Escherichia coli | - | pronounced reduction of affinity for pyrroloquinoline quinone, very weak activity of phenazine methosulfate reductase but still retains glucose oxidase activity equivalent to that of the wild-type | 639208 |
| Q126E | Sorangium cellulosum | - | the mutant shows 25.6% relative activity on maltose | 713001 |
| Q126R | Sorangium cellulosum | - | the mutant shows 11.4% relative activity on maltose | 713001 |
| Q126S | Sorangium cellulosum | - | the mutant shows 12.4% relative activity on maltose | 713001 |
| Q219E/F220E | Sorangium cellulosum | - | the mutant shows 5.2% relative activity on maltose | 713001 |
| Q219K/F220C | Sorangium cellulosum | - | the mutant shows 20% relative activity on maltose | 713001 |
| Q219K/F220K | Sorangium cellulosum | - | the mutant shows 29.3% relative activity on maltose | 713001 |
| Q219N/F220K | Sorangium cellulosum | - | the mutant shows 11.7% relative activity on maltose | 713001 |
| M367P/A376T | Acinetobacter calcoaceticus | P13650 | mutant, relative activity vs wild type, substrate glucose 0.65, substrate maltose 0.24 | 671548 |
| additional information | Acinetobacter calcoaceticus | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus 25001 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus 25001 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus 25001 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus 25001 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus 69 V | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus 69 V | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus 69 V | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus 69 V | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus 69-V | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus 69-V | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus 69-V | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus 69-V | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus 80-1 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus 80-1 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus 80-1 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus 80-1 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus AC3 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus AC3 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus AC3 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus AC3 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus ADP-96 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus ADP-96 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus ADP-96 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus ADP-96 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus ATCC23055 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus ATCC23055 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus ATCC23055 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus ATCC23055 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus BADO ADP1 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus BADO ADP1 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus BADO ADP1 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus BADO ADP1 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus BD 413 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus BD 413 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus BD 413 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus BD 413 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus BD413 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus BD413 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus BD413 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus BD413 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus EBF | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus EBF | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus EBF | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus EBF | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus EGB | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus EGB | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus EGB | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus EGB | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus F45 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus F45 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus F45 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus F45 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus F46 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus F46 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus F46 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus F46 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus L.M.D. | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus L.M.D. | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus L.M.D. | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus L.M.D. | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus LMD 79.41 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus LMD 79.41 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus LMD 79.41 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus LMD 79.41 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus LMD79.41 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus LMD79.41 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus LMD79.41 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus LMD79.41 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus MdcH | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus MdcH | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus MdcH | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus MdcH | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus N.C.I.B. 8250 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus N.C.I.B. 8250 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus N.C.I.B. 8250 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus N.C.I.B. 8250 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus NCIM 2890 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus NCIM 2890 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus NCIM 2890 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus NCIM 2890 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus NCIMB 9871 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus NCIMB 9871 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus NCIMB 9871 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus NCIMB 9871 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus SW1 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus SW1 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus SW1 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus SW1 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| K166E | Acinetobacter calcoaceticus ULA-501 | - | site-directed mutagenesis, substrate binding residue mutation, altered substrate specificty compared to the wild-type enzyme | 654947 |
| additional information | Acinetobacter calcoaceticus ULA-501 | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Acinetobacter calcoaceticus ULA-501 | - | the recombinant cytochrome c-fusion protein shows a highly increased sensitivity when immobilized to the electrode as D-glucose sensor compared to the wild-type enzyme, overview | 654449 |
| additional information | Acinetobacter calcoaceticus ULA-501 | - | engineering PQQ glucose dehydrogenase with improved substrate specificity | 654947 |
| L712W | Escherichia coli | - | no GDH activity | 712800 |
| additional information | Escherichia coli | - | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | 639205 |
| additional information | Escherichia coli | - | construction of a gene consisting of two identical subunits linked together by a DNA segment coding linker peptide region and production of a linked-dimeric enzyme, the linked-dimeric enzyme shows higher thermal stability than native dimeric enzyme | 639212 |
| additional information | Escherichia coli | - | co-expression of peptide ligands in a random phage diplay modifies the substrate specificity of the enzyme towards mono- and disaccharides, overview | 655101 |
| additional information | Escherichia coli | - | studies on mGDH mutants with substitutions for amino acid residues around pyrroloquinoline quinone show that Asp-466 and Lys-493, which are crucial for catalytic activity, interact with bound ubiquinone. It is proposed that the bound ubiquinone is involved in the catalytic reaction in addition to the intramolecular electron transfer in mGDH | 702498 |
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