PedE does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome
Substrates: the unusual disulfide ring between the adjacent cysteine residues C105 and C106 is essential for efficient electron transfer at pH 7 from quinoprotein ethanol dehydrogenase to its natural electron acceptor cytochrome c550 Products: -
Substrates: PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome Products: -
Substrates: the unusual disulfide ring between the adjacent cysteine residues C105 and C106 is essential for efficient electron transfer at pH 7 from quinoprotein ethanol dehydrogenase to its natural electron acceptor cytochrome c550 Products: -
Substrates: PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome Products: -
PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GAGNPG in PedE, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster
PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GLGVQG and GSGVLG in PedH, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster
the enzymatic activity of the mutant enzyme in the artificial dye test with N-methylphenazonium methyl sulfate (PMS) and 2,6-dichlorophenol indophenol (DCPIP) at pH 9 does not depend on an activating amine which is essential for wild type activity under these condition
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 1-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
substrate: ethanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 1,3-propanediol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 1,3-propanediol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
substrate: 1-butanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
substrate: 1-butanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 1-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 2-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
substrate: 2-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
substrate: ethanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
all pyrroloquinoline quinone-dependent alcohol dehydrogenases contain an unusual disulfide ring formed between adjacent cysteine residues. A mutant enzyme that is lacking this structure is generated by replacing Cys105 and Cys106 with Ala. Heterologously expressed C105A/C106A apoenzyme is successfully converted to enzymatic active holo-enzyme by incorporation of its cofactor pyrroloquinoline quinone (PQQ) in the presence of Ca2+. The enzymatic activity of the mutant enzyme in the artificial dye test with N-methylphenazonium methyl sulfate (PMS) and 2,6-dichlorophenol indophenol (DCPIP) at pH 9 does not depend on an activating amine which is essential for wild type activity under these conditions. The mutant enzyme shows increased Michaelis constants for primary alcohols, while the affinity for the secondary alcohol 2-propanol is unaltered. For all substrates tested the specific activity of the mutant enzyme in the artificial dye test is higher than that found for wild type enzyme. In the ferricyanide test with the natural electron acceptor cytochrome c550 the activity of mutant Cys105Ala/Cys106Ala is 15fold lower than that of wild type enzyme
Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.
Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U
A soluble two-component regulatory system controls expression of quinoprotein ethanol dehydrogenase (QEDH) but not expression of cytochrome c(550) of the ethanol-oxidation system in Pseudomonas aeruginosa
Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550