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Literature summary for 1.14.13.92 extracted from

  • Bocola, M.; Schulz, F.; Leca, F.; Vogel, A.; Fraaije, M.W.; Reetz, M.T.
    Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: towards practical Baeyer-Villiger monooxygenases (2005), Adv. Synth. Catal., 347, 979-986.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
PAMO crystal structure analysis, comparison to cyclohexanone monooxygenase, EC 1.14.13.22 Thermobifida fusca

Protein Variants

Protein Variants Comment Organism
additional information construction of three mutants P1-P3 by elimination of a bulge loop region, involving residues Ser441, Ala442, and Leu443, leading to enhanced substrate enantioselectivity of Baeyer-Villiger reactions while maintaining high thermal stability, overview Thermobifida fusca

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.059
-
phenylacetone wild-type enzyme Thermobifida fusca
0.07
-
2-phenylcyclohexanone mutant P3 Thermobifida fusca
0.5
-
2-phenylcyclohexanone mutant P2 Thermobifida fusca
2.3
-
2-phenylcyclohexanone mutant P1 Thermobifida fusca
2.5
-
phenylacetone mutant P3 Thermobifida fusca
3
-
phenylacetone mutant P1 Thermobifida fusca
4
-
phenylacetone mutant P2 Thermobifida fusca

Organism

Organism UniProt Comment Textmining
Thermobifida fusca
-
a moderately thermophilic bacterium
-

Reaction

Reaction Comment Organism Reaction ID
phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O reaction mechanism Thermobifida fusca

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
additional information
-
-
Thermobifida fusca

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-methylphenylcyclohexanone + NADPH + O2 mutant P3 prefers the R-isomer Thermobifida fusca 7-benzyloxepan-2-one + NADP+ + H2O
-
?
2-phenylcyclohexanone + NADPH + O2 molecular modeling of the Criegee intermediate, the wild-type enzyme prefers the S-isomer, while mutants P1-P3 all prefer the R-isomer Thermobifida fusca 7-phenyloxepan-2-one + NADP+ + H2O
-
?
4-phenylcyclohexanone + NADPH + O2
-
Thermobifida fusca 4-phenyl-hexano-6-lactone + NADP+ + H2O
-
?
additional information substrate selectivity and stereospecificity of wild-type and mutant enzymes, overview Thermobifida fusca ?
-
?
phenylacetone + NADPH + H+ + O2
-
Thermobifida fusca benzyl acetate + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
More structure analysis, the enzyme exhibits a two-domain architecture, and a bulge loop region Thermobifida fusca

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the Baeyer-Villiger monooxygenases Thermobifida fusca
PAMO
-
Thermobifida fusca

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Thermobifida fusca

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.22
-
phenylacetone mutant P3 Thermobifida fusca
0.25
-
phenylacetone mutant P1 Thermobifida fusca
0.25
-
2-phenylcyclohexanone mutant P3 Thermobifida fusca
0.31
-
2-phenylcyclohexanone mutant P1 Thermobifida fusca
0.4
-
phenylacetone mutant P2 Thermobifida fusca
0.5
-
2-phenylcyclohexanone mutant P2 Thermobifida fusca
1.9
-
phenylacetone wild-type enzyme Thermobifida fusca

Cofactor

Cofactor Comment Organism Structure
FAD binding structure involving Arg337, overview Thermobifida fusca
NADPH
-
Thermobifida fusca