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Literature summary extracted from

  • Eiben, S.; Kaysser, L.; Maurer, S.; Kuehnel, K.; Urlacher, V.B.; Schmid, R.D.
    Preparative use of isolated CYP102 monooxygenases - a critical appraisal (2006), J. Biotechnol., 124, 662-669.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.14.14.1 synthesis the enzyme is intersting for regioselective production of compounds Bacillus subtilis
1.14.14.1 synthesis the enzyme is intersting for regioselective production of compounds Priestia megaterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.1 expression in Escherichia coli in fed-batch fermentation Bacillus subtilis
1.14.14.1 expression in Escherichia coli in fed-batch fermentation Priestia megaterium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.1 crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain Priestia megaterium

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.1 A74E/F87V/P386S site-directed mutagenesis, the mutant shows altered regioselectivity and activity, and cofactor specificity compared to the wild-type mutant Priestia megaterium
1.14.14.1 A74G/F87V/L188Q site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant Priestia megaterium
1.14.14.1 A74G/F87V/L188Q/R966D site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme Priestia megaterium
1.14.14.1 A74G/F87V/L188Q/R966M site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme Priestia megaterium
1.14.14.1 A74G/F87V/L188Q/S965D site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme Priestia megaterium
1.14.14.1 A74G/F87V/L188Q/W1046A site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme Priestia megaterium
1.14.14.1 A74G/F87V/L188Q/W1046S site-directed mutagenesis, the mutant shows altered kinetics, and cofactor specificity compared to the wild-type enzyme Priestia megaterium
1.14.14.1 F87G site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant Priestia megaterium
1.14.14.1 F87GA site-directed mutagenesis, the mutant shows altered regioselectivity and activity compared to the wild-type mutant Priestia megaterium
1.14.14.1 additional information construction of an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH Priestia megaterium

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.1 H2O2 at high concentrations Priestia megaterium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.1 0.002
-
NADPH mutants A74G/F87V/L188Q/W1046A and A74G/F87V/L188Q/W1046S Priestia megaterium
1.14.14.1 0.0025
-
NADPH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 0.004
-
NADH mutant A74G/F87V/L188Q/S965D Priestia megaterium
1.14.14.1 0.004
-
NADH mutant enzyme A74G/F87V/L188Q/W1046A/S965D, pH and temperature not specified in the publication Priestia megaterium
1.14.14.1 0.01
-
NADH mutant A74G/F87V/L188Q/W1046S Priestia megaterium
1.14.14.1 0.01
-
NADH mutant enzyme A74G/F87V/L188Q/W1046S, pH and temperature not specified in the publication Priestia megaterium
1.14.14.1 0.02
-
NADPH mutant A74G/F87V/L188Q/S965D Priestia megaterium
1.14.14.1 0.02
-
NADH mutant A74G/F87V/L188Q/W1046A Priestia megaterium
1.14.14.1 0.02
-
NADH mutant enzyme A74G/F87V/L188Q/W1046A, pH and temperature not specified in the publication Priestia megaterium
1.14.14.1 0.05
-
NADPH mutant A74G/F87V/L188Q/R966M Priestia megaterium
1.14.14.1 0.13
-
NADPH mutant A74G/F87V/L188Q/R966D Priestia megaterium
1.14.14.1 0.33
-
NADH mutant A74G/F87V/L188Q/R966D Priestia megaterium
1.14.14.1 0.33
-
NADH mutant enzyme A74G/F87V/L188Q/R966D, pH and temperature not specified in the publication Priestia megaterium
1.14.14.1 0.54
-
NADH mutant A74G/F87V/L188Q/R966M Priestia megaterium
1.14.14.1 0.54
-
NADH mutant enzyme A74G/F87V/L188Q/R966M, pH and temperature not specified in the publication Priestia megaterium
1.14.14.1 1.43
-
NADH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 1.43
-
NADH mutant enzyme A74G/F87V/L188Q, pH and temperature not specified in the publication Priestia megaterium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.14.1 Fe2+ a heme-containing P450 monooxygenase Bacillus subtilis
1.14.14.1 Fe2+ a heme-containing P450 monooxygenase Priestia megaterium

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.1 Bacillus subtilis
-
-
-
1.14.14.1 Priestia megaterium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.1 several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes Bacillus subtilis
1.14.14.1 several purification protocols are published, based on ion exchange chromatography, hydrophobic interaction chromatography or metal affinity chromatography, resulting in high levels of purity depending on the further application of the enzymes Priestia megaterium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.1 beta-ionone + [reduced NADPH-hemoprotein reductase] + O2
-
Priestia megaterium 4-hydroxy-beta-ionone + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
1.14.14.1 cytochrome c + NADH + H+ + O2
-
Priestia megaterium ?
-
r
1.14.14.1 cytochrome c + O2 + NADH
-
Priestia megaterium ?
-
r
1.14.14.1 additional information activity involves cytochrome c reduction, CYP102A1 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions, an engineered CYP102A1 heme domain which utilizes H2O2 as electron donor Priestia megaterium ?
-
?
1.14.14.1 additional information activity involves cytochrome c reduction, CYP102A3 hydroxylates and epoxidizes middle to long chain saturated, unsaturated and branched fatty acids at subterminal positions Bacillus subtilis ?
-
?
1.14.14.1 styrene + O2 + H2O2 engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH Priestia megaterium (R)-styrene oxide + (S)-styrene oxide + H2O
-
?
1.14.14.1 styrene + O2 + NAD(P)H
-
Priestia megaterium (R)-styrene oxide + (S)-styrene oxide + H2O + NAD(P)+ enantioselective styrene oxidation with different CYP102A1 mutants, 25% S-isomer for the wild-type enzyme, 58% S-isomer for mutant A74E/F87V/P386S, 49% R-isomer for mutant F87A, 65% R-isomer for mutant A74G/F87V/L188Q, and 92% R-isomer for mutant F87G ?

Subunits

EC Number Subunits Comment Organism
1.14.14.1 More the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain Bacillus subtilis
1.14.14.1 More the enzyme is a natural fusion enzyme composed of an N-terminal heme monooxygenase linked to the C-terminal diflavin reductase domain Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
1.14.14.1 CYP102 monooxygenase
-
Bacillus subtilis
1.14.14.1 CYP102 monooxygenase
-
Priestia megaterium
1.14.14.1 CYP102A1
-
Priestia megaterium
1.14.14.1 CYP102A3
-
Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.14.14.1 additional information
-
melting temperatures of the CYP102A1 monooxygenase and the CYP102A1 reductase domain differ by about 15°C: whereas Tm for the monooxygenase domain is 63°C, it is only 48°C for the reductase domain Priestia megaterium
1.14.14.1 46
-
10 min, half-life, wild-type CYP102A1 Priestia megaterium
1.14.14.1 61
-
10 min, half-life, engineered CYP102A1 heme domain which utilizes H2O2 as electron donor Priestia megaterium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.1 0.016
-
NADH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 0.43
-
NADPH mutant F87A Priestia megaterium
1.14.14.1 0.45
-
NADPH wild-type enzyme Priestia megaterium
1.14.14.1 0.5
-
NADPH mutant F87G Priestia megaterium
1.14.14.1 0.83
-
NADPH mutant A74E/F87V/P386S Priestia megaterium
1.14.14.1 1.7
-
NADPH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 5.67
-
NADPH mutant A74G/F87V/L188Q/S965D Priestia megaterium
1.14.14.1 6.5
-
NADPH mutant A74G/F87V/L188Q/W1046A Priestia megaterium
1.14.14.1 7
-
NADH mutant A74G/F87V/L188Q/S965D Priestia megaterium
1.14.14.1 9.3
-
NADPH mutant A74G/F87V/L188Q/R966M Priestia megaterium
1.14.14.1 9.83
-
NADPH mutant A74G/F87V/L188Q/W1046S Priestia megaterium
1.14.14.1 32
-
NADH mutant A74G/F87V/L188Q/R966D Priestia megaterium
1.14.14.1 37.83
-
NADH mutant A74G/F87V/L188Q/R966M Priestia megaterium
1.14.14.1 46.83
-
NADH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 89
-
NADH mutant A74G/F87V/L188Q/W1046A Priestia megaterium
1.14.14.1 105.2
-
NADH mutant A74G/F87V/L188Q/W1046A Priestia megaterium
1.14.14.1 132.2
-
NADPH mutant A74G/F87V/L188Q Priestia megaterium
1.14.14.1 156
-
NADH mutant A74G/F87V/L188Q/W1046S Priestia megaterium
1.14.14.1 183
-
NADPH mutant A74G/F87V/L188Q/R966D Priestia megaterium
1.14.14.1 362.8
-
NADPH mutant A74G/F87V/L188Q/R966M Priestia megaterium

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.1 cytochrome c
-
Bacillus subtilis
1.14.14.1 cytochrome c
-
Priestia megaterium
1.14.14.1 FAD bound Bacillus subtilis
1.14.14.1 FAD bound, binding structure, overview Priestia megaterium
1.14.14.1 FMN bound Bacillus subtilis
1.14.14.1 FMN bound, binding structure, overview Priestia megaterium
1.14.14.1 additional information engineered CYP102A1 heme domain which utilizes H2O2 as electron donor instead of NADPH Priestia megaterium
1.14.14.1 additional information residues S965, R966 and Y974 are important in the Rossman fold-like binding motif for the cofactor binding and discrimination, overview Priestia megaterium
1.14.14.1 NAD(P)H
-
Priestia megaterium
1.14.14.1 NADPH
-
Bacillus subtilis