EC Number   |
Protein Variants |
Reference |
|---|
   1.1.2.8 | A26V |
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability |
725154 |
| 1.1.2.8 | C105A/C106A |
mutation of residues forming a characteristic disulfide ring in the binding pocket of pyrroloquinoline quinone. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone |
674560 |
| 1.1.2.8 | E408P |
mutant shows a 2.3fold increased stability upon incubation at 45°C for 1 h compared with the wild-type allele |
763436 |
| 1.1.2.8 | G55D |
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability |
725154 |
| 1.1.2.8 | L18Q |
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability |
725154 |
| 1.1.2.8 | more |
a triple mutant strain (mxaF xoxF1 xoxF2, named MDH-3), deficient in the three methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, is mutated in the MDH-3 background, the quadruple mutant strain can no longer grow on methanol in minimal medium with added lanthanum (La3+) |
-, 742793 |
| 1.1.2.8 | more |
construction of adhS gene disruptant and mutants. The adhS gene disruptant completely loses its PQQ-ADH activity and acetate-producing ability but retains acetic acid toleration. In contrast, this disruptant grows well, even better than the wild-type, in the ethanol containing medium even though its PQQ-ADH activity and ethanol oxidizing ability is completely lost, while NAD+-dependent ADH is induced. Random mutagenesis of adhS gene reveal that complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affects neither the PQQ-ADH activity nor ethanol oxidizing ability, overview |
725154 |
| 1.1.2.8 | more |
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127 |
-, 743174 |
| 1.1.2.8 | more |
generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127 |
-, 743174 |
| 1.1.2.8 | more |
In the presence of the prosthetic group, expression of the Pseudomonas gene encoding the 60-kDa subunit of quinoprotein ethanol dehydrogenase in Escherichia coli results in formation of active enzyme |
389964 |
