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Literature summary for 1.14.14.1 extracted from

  • Lentz, O.; Urlacher, V.; Schmid, R.D.
    Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis (2004), J. Biotechnol., 108, 41-49.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dimethylsulfoxid up to 25% v/v Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
-
Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
A74G/F88V substrate specificity similar to wild-type Bacillus subtilis
A74G/F88V/S189Q substrate spectrum much broader than for wild-type Bacillus subtilis
A74G/S189Q substrate specificity similar to wild-type Bacillus subtilis

General Stability

General Stability Organism
not stable in NaCl above 150 mM Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0064
-
omega-(p-nitrophenyl)decanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis
0.0065
-
omega-(p-nitrophenyl)dodecanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis
0.0104
-
omega-(p-nitrophenyl)dodecanoic acid pH 8.0, wild-type Bacillus subtilis
0.0245
-
omega-(p-nitrophenyl)decanoic acid pH 8.0, wild-type Bacillus subtilis
0.0319
-
omega-(p-nitrophenyl)octanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis
0.0618
-
omega-(p-nitrophenyl)octanoic acid pH 8.0, wild-type Bacillus subtilis

Organic Solvent Stability

Organic Solvent Comment Organism
DMSO stable, and activity increases in presence of up to 25% DMSO (v/v) Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
isozyme CYP102A3, natural fusion protein consisting of a heme domain and a reductase domain
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-ionone + [reduced NADPH-hemoprotein reductase] + O2 substrate only for mutant A74G/F88V/S189Q Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
capric acid + [reduced NADPH-hemoprotein reductase] + O2 about 10% of the activity with palmitic acid, wild-type Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
caprylic acid + [reduced NADPH-hemoprotein reductase] + O2 substrate only for mutant A74G/F88V/S189Q Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
-
Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
naphthalene + [reduced NADPH-hemoprotein reductase] + O2 substrate only for mutant A74G/F88V/S189Q Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
octane + [reduced NADPH-hemoprotein reductase] + O2 substrate only for mutant A74G/F88V/S189Q and for mutant A74G/S189Q Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
omega-(p-nitrophenyl)decanoic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
omega-(p-nitrophenyl)dodecanoic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
omega-(p-nitrophenyl)octanoic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
palmitic acid + [reduced NADPH-hemoprotein reductase] + O2
-
Bacillus subtilis ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.4
-
omega-(p-nitrophenyl)octanoic acid pH 8.0, wild-type Bacillus subtilis
1.3
-
omega-(p-nitrophenyl)dodecanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis
1.3
-
omega-(p-nitrophenyl)decanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis
1.5
-
omega-(p-nitrophenyl)decanoic acid pH 8.0, wild-type Bacillus subtilis
3.1
-
omega-(p-nitrophenyl)dodecanoic acid pH 8.0, wild-type Bacillus subtilis
3.5
-
omega-(p-nitrophenyl)octanoic acid pH 8.0, mutant A74G/F88V/S189Q Bacillus subtilis