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Literature summary for 1.14.14.11 extracted from

  • Riedel, A.; Heine, T.; Westphal, A.H.; Conrad, C.; Rathsack, P.; van Berkel, W.J.; Tischler, D.
    Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding (2015), AMB Express, 5, 112 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhodococcus opacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 isoform StyA2B constitutes dimers under reduced conditions Rhodococcus opacus
additional information
-
 StyA1 is a dimer in its active form, gel filtration Rhodococcus opacus

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus A0A076JVU4 styrene monooxygenase StyA
-
Rhodococcus opacus C7ACG0 and C7ACG1 i.e. oxygenase components StyA1 and StyA2B
-
Rhodococcus opacus C7ACG1
-
-
Rhodococcus opacus 1CP A0A076JVU4 styrene monooxygenase StyA
-
Rhodococcus opacus 1CP C7ACG0 and C7ACG1 i.e. oxygenase components StyA1 and StyA2B
-
Rhodococcus opacus 1CP C7ACG1
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.081
-
 substrate styrene, presence of FAD reductase StyB originated from Pseudomonas fluorescens ST, pH 7.5, 30°C Rhodococcus opacus
0.087
-
 substrate styrene, presence of FAD reductase StyB originated from Pseudomonas fluorescens ST, pH 7.5, 30°C Rhodococcus opacus
0.12
-
 substrate styrene, presence of FAD reductase StyB originated from Pseudomonas fluorescens ST, pH 7.5, 30°C Rhodococcus opacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl vinyl sulfide + FADH2 + O2
-
 Rhodococcus opacus (S)-phenyl vinyl sulfoxide + FAD + H2O
-
 ?
phenyl vinyl sulfide + FADH2 + O2
-
 Rhodococcus opacus 1CP (S)-phenyl vinyl sulfoxide + FAD + H2O
-
 ?
styrene + FADH2 + O2
-
 Rhodococcus opacus (S)-styrene oxide + FAD + H2O
-
 ?
styrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (S)-styrene oxide + FAD + H2O
-
 ?

Subunits

Subunits Comment Organism
dimer enzyme is active as a heterodimer with flavin oxidoreductase StyB. 1 * 46580, StyA, plus 1 * 19053, StyB, calculated, 1 * 50000, StyA plus 1 * 21500, StyB, SDS-PAGE of recombinant His-tagged proteins Rhodococcus opacus

Synonyms

Synonyms Comment Organism
StyA
-
 Rhodococcus opacus
StyA2B
-
 Rhodococcus opacus

Cofactor

Cofactor Comment Organism Structure
FAD incorporation of reduced FAD into StyA enzymes is attended with significant conformational rearrangements Rhodococcus opacus