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Literature summary for 1.14.14.11 extracted from

  • Otto, K.; Hofstetter, K.; Röthlisberger, M.; Witholt, B., Schmid, A.
    Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase (2004), J. Bacteriol., 186, 5292-5302.
    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 Pseudomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
FAD at a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
 Styrene pH 7.5, 37°C, recombinant enzyme Pseudomonas sp.
0.45
-
 Styrene pH 7.5, 37°C, wild-type enzyme Pseudomonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
additional information StyA does not contain Fe2+, Cu2+, Zn2+, Mn2+, Co2+, or Mg2+ Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46350
-
 2 * 46350, MALDI-TOF analysis Pseudomonas sp.
47000
-
 2 * 47000, SDS-PAGE Pseudomonas sp.
80000
-
 gel filtration Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
styrene + FADH2 + O2 Pseudomonas sp. the epoxidation of the vinyl side chain of styrene catalyzed by a monooxygenase is the initial reaction in one microbial aerobic styrene degradation pathway (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 Pseudomonas sp. VLB120 the epoxidation of the vinyl side chain of styrene catalyzed by a monooxygenase is the initial reaction in one microbial aerobic styrene degradation pathway (S)-2-phenyloxirane + FAD + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. VLB120
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.9
-
 pH 7.5, 37°C, wild-type StyA Pseudomonas sp.
2.1
-
 pH 7.5, 37°C, recombinant StyA Pseudomonas sp.

Storage Stability

Storage Stability Organism
4°C, addition of 10% v/v glycerol and 1 mM pefabloc to the storage buffer improves enzyme stability, the activity decreases by 20% during the first 2 weeks, StyA retains 60% of its initial activity after 3 months Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the wild-type enzyme catalyzes the epoxidation of p-, alpha-, and beta-methylstyrene, 1,2-dihydronaphthalene, methyl phenyl sulfide, and 3-chlorostyrene at rates comparable to those achieved with the recombinant form of the enzyme Pseudomonas sp. ?
-
 ?
additional information the wild-type enzyme catalyzes the epoxidation of p-, alpha-, and beta-methylstyrene, 1,2-dihydronaphthalene, methyl phenyl sulfide, and 3-chlorostyrene at rates comparable to those achieved with the recombinant form of the enzyme Pseudomonas sp. VLB120 ?
-
 ?
styrene + FADH2 + O2 the epoxidation of the vinyl side chain of styrene catalyzed by a monooxygenase is the initial reaction in one microbial aerobic styrene degradation pathway Pseudomonas sp. (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 styrene is exclusively converted to S-styrene oxide. During the epoxidation reaction, no formation of a complex of StyA and StyB is observed, suggesting that electron transport between reductase and oxygenase occurs via a diffusing flavin. StyA activity was strongly influenced by the amount of StyB added. No epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin Pseudomonas sp. (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 the epoxidation of the vinyl side chain of styrene catalyzed by a monooxygenase is the initial reaction in one microbial aerobic styrene degradation pathway Pseudomonas sp. VLB120 (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 styrene is exclusively converted to S-styrene oxide. During the epoxidation reaction, no formation of a complex of StyA and StyB is observed, suggesting that electron transport between reductase and oxygenase occurs via a diffusing flavin. StyA activity was strongly influenced by the amount of StyB added. No epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin Pseudomonas sp. VLB120 (S)-2-phenyloxirane + FAD + H2O
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 47000, SDS-PAGE Pseudomonas sp.
dimer 2 * 46350, MALDI-TOF analysis Pseudomonas sp.

Synonyms

Synonyms Comment Organism
StyA
-
 Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pseudomonas sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6
-
 Styrene pH 7.5, 37°C Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FADH2 no epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin. At a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases Pseudomonas sp.

pI Value

Organism Comment pI Value Maximum pI Value
Pseudomonas sp. calculated from sequence
-
 5.3