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Literature summary extracted from

  • Fordwour, O.B.; Wolthers, K.R.
    Active site variants provide insight into the nature of conformational changes that accompany the cyclohexanone monooxygenase catalytic cycle (2018), Arch. Biochem. Biophys., 654, 85-96 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.22 T187A elimination of the hydrogen bond to the phosphate of the nicotinamide mononucleotide half of NADP(H), 15fold reduction in turnover of cyclohexanone. Mutation does not affect the rate of FAD reduction or the coupling efficiency Acinetobacter sp.
1.14.13.22 W490F elimination of the hydrogen bond to the ribose of the nicotinamide mononucleotide half of NADP(H), 15fold reduction in turnover of cyclohexanone. Mutation does not affect the rate of FAD reduction or the coupling efficiency Acinetobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.22 Acinetobacter sp. P12015
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.22 cyclohexanone + NADPH + H+ + O2
-
 Acinetobacter sp. hexano-6-lactone + NADP+ + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.22 0.43
-
 cyclohexanone mutant T187A, pH 7.5, 25°C Acinetobacter sp.
1.14.13.22 0.43
-
 cyclohexanone mutant W490F, pH 7.5, 25°C Acinetobacter sp.
1.14.13.22 6.5
-
 cyclohexanone wild-type, pH 7.5, 25°C Acinetobacter sp.

General Information

EC Number General Information Comment Organism
1.14.13.22 metabolism residue T187 is critical for locking NADP+ in a configuration that dramatically accelerates O2 activation by the reduced flavin. W490 also promotes O2 activation (albeit less so than T187) and accelerates the reaction between the C4a-peroxyflavin and cyclohexanone Acinetobacter sp.