Difference between revisions of "Part:BBa K3853001"

Latest revision as of 14:19, 12 October 2021

Aryl alcohol oxidase (AAO)

Aryl alcohol oxidase (AAO), a member of the glucose-methanol-choline oxidase / dehydrogenase (GMC) superfamily, is an enzyme containing flavin-adenine-dinucleotide (FAD) that catalyze the oxidation of aromatic and aliphatic allylic primary alcohols to the corresponding aldehydes while reducing molecular oxygen to H₂O₂.This gene comes from Pleurotus eryngii. Using the Thermo GeneArt online tool geneoptimize, we optimize the codon of the protein gene sequence to improve its expression in Pichia pastoris. The introduction of this gene as a H₂O₂-producing enzyme to assist MnP to play its role.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 525
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 238
Illegal BamHI site found at 1237
Illegal BamHI site found at 1624
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K3853001 short</partinfo>
-Aryl alcohol oxidase (AAO), a member of the glucose-methanol-choline oxidase / dehydrogenase (GMC) superfamily, is an enzyme containing flavin-adenine-dinucleotide (FAD) that catalyze the oxidation of aromatic and aliphatic allylic primary alcohols to the corresponding aldehydes while reducing molecular oxygen to H<sub>2</sub>O<sub>2</sub>.This gene comes from <i>Pleurotus eryngii</i>. Using the <b>Thermo GeneArt</b> online tool geneoptimize, we optimize the codon of the protein gene sequence to improve its expression in <i>Pichia pastoris</i>. The introduction of this gene as a H<sub>2</sub>O<sub>2</sub>-producing enzyme to assist MnP to play its role. 123
+Aryl alcohol oxidase (AAO), a member of the glucose-methanol-choline oxidase / dehydrogenase (GMC) superfamily, is an enzyme containing flavin-adenine-dinucleotide (FAD) that catalyze the oxidation of aromatic and aliphatic allylic primary alcohols to the corresponding aldehydes while reducing molecular oxygen to H<sub>2</sub>O<sub>2</sub>.This gene comes from <i>Pleurotus eryngii</i>. Using the <b>Thermo GeneArt</b> online tool geneoptimize, we optimize the codon of the protein gene sequence to improve its expression in <i>Pichia pastoris</i>. The introduction of this gene as a H<sub>2</sub>O<sub>2</sub>-producing enzyme to assist MnP to play its role.
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