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Literature summary for 1.14.13.16 extracted from

  • Carvalho, A.T.P.; Dourado, D.F.A.R.; Skvortsov, T.; de Abreu, M.; Ferguson, L.J.; Quinn, D.J.; Moody, T.S.; Huang, M.
    Spatial requirement for PAMO for transformation of non-native linear substrates (2018), Phys. Chem. Chem. Phys., 20, 2558-2570 .
    View publication on PubMed
Search for more literature for 1.14.13.16

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetic analysis of the mutant enzyme Thermobifida fusca
0.25
-
 2-Octanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
0.8
-
 2-phenylcyclohexanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
1000
-
 Cyclopentanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclopentanone + NADPH + H+ + O2 Thermobifida fusca
-
 5-valerolactone + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Thermobifida fusca
-
 phenylacetone monooxygenase enzyme mutant P253F/G254A/R258M/L443F
-

Reaction

Reaction Comment Organism Reaction ID
cyclopentanone + NADPH + H+ + O2 = 5-valerolactone + NADP+ + H2O the reaction mechanism of BVMO with native substrate phenylacetone proceeds via the formation of a Criegee intermediate with anionic character, which is subsequently rearranged via the migration of alkyl group to yield the product ester, reaction mechanism, overview Thermobifida fusca
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-octanone + NADPH + H+ + O2
-
 Thermobifida fusca heptylacetate + NADP+ + H2O
-
 ?
2-phenylcyclohexanone + NADPH + H+ + O2 high activity with PAMO enzyme mutant P253F/G254A/R258M/L443F, almost no activity with wild-type PAMO (EC 1.14.13.92) Thermobifida fusca ? + NADP+ + H2O
-
 ?
cyclopentanone + NADPH + H+ + O2
-
 Thermobifida fusca 5-valerolactone + NADP+ + H2O
-
 ?
cyclopentanone + NADPH + H+ + O2 high activity with PAMO enzyme mutant P253F/G254A/R258M/L443F, almost no activity with wild-type PAMO (EC 1.14.13.92) Thermobifida fusca 5-valerolactone + NADP+ + H2O
-
 ?
additional information the engineered phenylacetone monooxygenase (EC 1.14.13.92) enzyme mutant P253F/G254A/R258M/L443F has almost lost its activity with phenylacetone, but shows higher activity with cyclopentanone instead. Substrate binding analysis, overview Thermobifida fusca ?
-
-

Synonyms

Synonyms Comment Organism
CPMO
-
 Thermobifida fusca
More cf. EC 1.14.13.92 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
0.3
-
 2-phenylcyclohexanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
1.6
-
 Cyclopentanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
2.3
-
 2-Octanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Thermobifida fusca

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Thermobifida fusca
NADPH
-
 Thermobifida fusca

General Information

General Information Comment Organism
evolution the enzyme belongs to the group I of Baeyer-Villiger monooxygenases (BMVOs) Thermobifida fusca
additional information enzyme molecular docking and molecular dynamics, computational modeling, overview Thermobifida fusca

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0016
-
 Cyclopentanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
0.375
-
 2-phenylcyclohexanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca
9.2
-
 2-Octanone recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C Thermobifida fusca