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Literature summary for 1.14.13.16 extracted from

  • Clouthier, C.M.; Kayser, M.M.; Reetz, M.T.
    Designing new Baeyer-Villiger monooxygenases using restricted CASTing (2006), J. Org. Chem., 71, 8431-8437.
    View publication on PubMed
Search for more literature for 1.14.13.16

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutants in strains BL121(DE3) and JM109 Acinetobacter sp.

Protein Variants

Protein Variants Comment Organism
additional information mutations in the active site residues responsible for stereoselectivity is a shortcut to an improvement in enantioselectivity in the often unselective CPMO, the combination of rational design and random mutagenesis at the predefined positions gives rise to focused libraries for improvement of the catalytic performance of enzymes, including enhanced enantioselectivity, using Complete Active Site Saturation Test, CAST, overview Acinetobacter sp.

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Acinetobacter sp.
-
-
-
Acinetobacter sp. NCIB 9871
-
-
-

Reaction

Reaction Comment Organism Reaction ID
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O reaction mechanism via key intermediate flavin C4a-peroxide, involving the four-electron reduction of O2 at the expense of a two-electron oxidation of NADPH and a two-electron oxidation of cyclohexanone to epsilon-caprolactone, overview Acinetobacter sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-acetoxy-cyclohexanone + NADPH + O2 low enantioselectivity Acinetobacter sp. 4-acetoxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-acetoxy-cyclohexanone + NADPH + O2 low enantioselectivity Acinetobacter sp. NCIB 9871 4-acetoxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-hydroxy-cyclohexanone + NADPH + O2 high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity Acinetobacter sp. 4-hydroxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-hydroxy-cyclohexanone + NADPH + O2 high enantioselectivity with 85% formation of the S-isomer, Ser450 is responsible for the high stereoselectivity Acinetobacter sp. NCIB 9871 4-hydroxy-hexano-6-lactone + NADP+ + H2O
-
 ?
4-methyl-cyclohexanone + NADPH + O2 low enantioselectivity Acinetobacter sp. 4-methyl-hexano-6-lactone + NADP+ + H2O
-
 ?
4-methyl-cyclohexanone + NADPH + O2 low enantioselectivity Acinetobacter sp. NCIB 9871 4-methyl-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, overview, 4-tert-butylcyclohexanone is a no substrate Acinetobacter sp. ?
-
 ?
additional information the enzyme acts as Baeyer-Villiger monooxygenase, substrate specificity and enantioselectivity, overview, 4-tert-butylcyclohexanone is a no substrate Acinetobacter sp. NCIB 9871 ?
-
 ?

Subunits

Subunits Comment Organism
More sequence alignment, and structure modelling and comparison to cyclophexanone monooxygenase, EC 1.14.13.22, structure-function analysis Acinetobacter sp.

Synonyms

Synonyms Comment Organism
CPMO
-
 Acinetobacter sp.
More cf. EC 1.14.13.22, the enzyme belongs to a class of bacterial flavoprotein monooxygenases Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
FAD bound Acinetobacter sp.
NADPH
-
 Acinetobacter sp.