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Results 1 - 10 of 14 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5A26V random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability -, 725154
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5F412I/W561Q wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.35 U/mg) 762532
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5F412I/W561S wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.12 U/mg) 762532
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5F412V/W561A wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows activity (1.04 U/mg). The mutant enzyma slso The KM-value for ethanol is approximately 525fold higher than that the wild-type value, whereas the maximal velocity is unchanged. This suggests that the oxidative capability of the PedHF412V/W561A variant is unaffected by the amino acid changes, and only the substrate binding is modulated 762532
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5G55D random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability -, 725154
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5L18Q random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability 725154
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5more construction of enzyme electrodes containing pyrroloquinoline quinone-dependent alcohol dehydrogenase as a biological component in combination with 4-ferrocenylphenol as an electron transfer mediator between PQQ and a carbon electrode for measurements of ethanol, overview. The biosensor shows the highest response at pH 5.5 and the working potential of 0.3 V, versus AgNAgCl, for ADH -, 686376
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5more disruption of genes exaA2 and exaA3 -, 726014
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5more random mutagenesis of adhS gene, complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking of the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affected neither the PQQ-ADH activity nor ethanol oxidizing ability -, 725154
Display the word mapDisplay the reaction diagram Show all sequences 1.1.5.5T104K random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability 725154
Results 1 - 10 of 14 > >>