Cloned (Comment) | Organism |
---|---|
overexpression of wild-type and mutant enzymes in Escherichia coli | Acinetobacter sp. |
Protein Variants | Comment | Organism |
---|---|---|
F156H/G157L | site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme | Acinetobacter sp. |
F156L/G157F | site-directed mutagenesis, the mutations improve the hydrophobic active site pocket increasing enzyme selectivity and stereospecificity | Acinetobacter sp. |
F156N/G157Y | site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme | Acinetobacter sp. |
F450C | site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme | Acinetobacter sp. |
F450I | site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme | Acinetobacter sp. |
G119S/F450Y | site-directed mutagenesis, the mutant shows altered substrate specificity and stereoselectivity compared to the wild-type enzyme | Acinetobacter sp. |
additional information | active site mutations to improve enantioselectivity of the enzyme towards 4-substituted cyclohexanone substrates, method evaluation, overview, the effect of mutation of residues 449 and 450 does not have a full impact on the improvement of the hydrophobic pocket | Acinetobacter sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cyclopentanone + NADPH + O2 | Acinetobacter sp. | - |
5-valerolactone + NADP+ + H2O | - |
? | |
cyclopentanone + NADPH + O2 | Acinetobacter sp. NCIB 9871 | - |
5-valerolactone + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter sp. | - |
- |
- |
Acinetobacter sp. NCIB 9871 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O | residues Phe450 and Phe156 are important for reaction stereospecificity | Acinetobacter sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-acetoxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-acetoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-acetoxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. NCIB 9871 | 4-acetoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-allyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-allyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-allyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. NCIB 9871 | 4-allyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-ethoxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-ethoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-ethyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-ethyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-hydroxy-4-allyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | ? | - |
? | |
4-hydroxy-4-ethyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | ? | - |
? | |
4-hydroxy-4-methyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | ? | - |
? | |
4-hydroxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-hydroxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-hydroxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. NCIB 9871 | 4-hydroxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-methoxy-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-methoxy-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-methyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-methyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
4-n-propyl-cyclohexanone + NADPH + O2 | - |
Acinetobacter sp. | 4-n-propyl-hexano-6-lactone + NADP+ + H2O | - |
? | |
cyclopentanone + NADPH + O2 | - |
Acinetobacter sp. | 5-valerolactone + NADP+ + H2O | - |
? | |
cyclopentanone + NADPH + O2 | - |
Acinetobacter sp. NCIB 9871 | 5-valerolactone + NADP+ + H2O | - |
? | |
additional information | the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity of wild-type and mutant enzymes, structure-function analysis and comparison to cyclohexanone monooxygenase, EC 1.14.13.22, residues Phe450 and Phe156 are important, overview | Acinetobacter sp. | ? | - |
? | |
additional information | the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity of wild-type and mutant enzymes, structure-function analysis and comparison to cyclohexanone monooxygenase, EC 1.14.13.22, residues Phe450 and Phe156 are important, overview | Acinetobacter sp. NCIB 9871 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CPMO | - |
Acinetobacter sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | bound | Acinetobacter sp. | |
NADPH | - |
Acinetobacter sp. |