substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
the enzyme is a member of the hydrolyase enzyme group. Hydro-lyases are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
the enzyme contains four typical consensus sequences for N-linked glycosylation. The temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
the enzyme contains four typical consensus sequences for N-linked glycosylation. The temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, higher functional recombinant expression of codon-harmonized gene encoding the enzyme in Pichia pastoris (i.e. Komagataella phaffii) strain CBS7435 as C-terminally His10-tagged protein, the mature enzyme is secreted. Upscaling tests show that Pichia pastoris is a most appropriate host for producing high amounts of recombinant NhKHS
DNA and amino acid sequence determination and analysis, sequence comparisons, lower functional recombinant expression of codon-harmonized gene encoding the enzyme in Pichia pastoris (i.e. Komagataella phaffii) strain CBS7435 as C-terminally His10-tagged protein
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds. The compatibility of enzyme NhKHS with nonpolar organic solvents is beneficial for a number of biocatalytic applications, e.g. in general for conversion of hydrophobic substrates
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds. The compatibility of enzyme NhKHS with nonpolar organic solvents is beneficial for a number of biocatalytic applications, e.g. in general for conversion of hydrophobic substrates
Engleder, M.; Horvat, M.; Emmerstorfer-Augustin, A.; Wriessnegger, T.; Gabriel, S.; Strohmeier, G.; Weber, H.; Mueller, M.; Kaluzna, I.; Mink, D.; Schuermann, M.; Pichler, H.
Recombinant expression, purification and biochemical characterization of kievitone hydratase from Nectria haematococca