Literature summary for 1.14.13.22 extracted from

Kohl, A.; Srinivasamurthy, V.; Boettcher, D.; Kabisch, J.; Bornscheuer, U.T.
Co-expression of an alcohol dehydrogenase and a cyclohexanone monooxygenase for cascade reactions facilitates the regeneration of the NADPH cofactor (2018), Enzyme Microb. Technol., 108, 53-58 .

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Cloned(Commentary)

Cloned (Comment)	Organism
dual expression of alcohol dehydrogenase (from Lactobacillus kefir) and cyclohexanone monooxygenase is achieved in Escherichia coli. Investigation of an approach for optimization of a whole-cell multi-enzyme cascade reaction by applying co-expression of the required cascade enzymes. Using the co-expression strategy, higher conversion values are obtained in whole-cell biocatalysis compared to expression of the cyclohexanone monooxygenase and alcohol dehydrogenase in individual Escherichia coli cells	Acinetobacter sp.

Cloned (Comment)

Organism

dual expression of alcohol dehydrogenase (from Lactobacillus kefir) and cyclohexanone monooxygenase is achieved in Escherichia coli. Investigation of an approach for optimization of a whole-cell multi-enzyme cascade reaction by applying co-expression of the required cascade enzymes. Using the co-expression strategy, higher conversion values are obtained in whole-cell biocatalysis compared to expression of the cyclohexanone monooxygenase and alcohol dehydrogenase in individual Escherichia coli cells

Acinetobacter sp.

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter sp.	Q9R2F5	-	-
Acinetobacter sp. NCIMB 9871	Q9R2F5	-	-

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Release 2023.1 (January 2023)