Difference between revisions of "Part:BBa K2271115"

Revision as of 14:59, 30 October 2017

ADH alcohol dehydrogenase

The ADH we used for our project is from Pichia pastoris. It converts (+)-trans-nootkatol into (+)-nootkatone by oxidation, using NAD+ as a cofactor. Usually an additionally cofactor regeneration is not necessary, as BM3 degrades NADH+H+ into NAD+ and ADH regenerates it. But because of the improved (+)-nootkatone producing function of BM3, another cofactor regenerating enzyme is necessary. In recent studies it was shown that Glucose Dehydrogenases (GDH) are appropriate enzymes for this attempt.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal suffix found in sequence at 2047
Illegal BglII site found at 880
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 2402
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K2271115 short</partinfo>
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+The ADH we used for our project is from Pichia pastoris.
+It converts (+)-trans-nootkatol into (+)-nootkatone by oxidation, using NAD+ as a cofactor. Usually an additionally cofactor regeneration is not necessary, as BM3 degrades NADH+H+ into NAD+ and ADH regenerates it.
+But because of the improved (+)-nootkatone producing function of BM3, another cofactor regenerating enzyme is necessary. In recent studies it was shown that Glucose Dehydrogenases (GDH) are appropriate enzymes for this attempt.
 <!-- Add more about the biology of this part here