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Literature summary extracted from

  • Tischler, D.; Kermer, R.; Groening, J.A.; Kaschabek, S.R.; van Berkel, W.J.; Schloemann, M.
    StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system (2010), J. Bacteriol., 192, 5220-5227.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.11 functional expression of His10-StyA2B in Escherichia coli Rhodococcus opacus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.11 44000
-
 2 * 44000, SDS-PAGE Rhodococcus opacus
1.14.14.11 80000
-
 gel filtration Rhodococcus opacus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.11 styrene + FADH2 + O2 Rhodococcus opacus
-
 (S)-2-phenyloxirane + FAD + H2O
-
 ?
1.14.14.11 styrene + FADH2 + O2 Rhodococcus opacus 1CP
-
 (S)-2-phenyloxirane + FAD + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.11 Rhodococcus opacus C7ACG0 StyA1
-
1.14.14.11 Rhodococcus opacus 1CP C7ACG0 StyA1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.11
-
 Rhodococcus opacus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.11 2-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 2-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 3-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 3-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 4-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 4-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
-
 ?
1.14.14.11 4-methylstyrene + FADH2 + O2
-
 Rhodococcus opacus ? + FAD + H2O
-
 ?
1.14.14.11 styrene + FADH2 + O2
-
 Rhodococcus opacus (S)-2-phenyloxirane + FAD + H2O
-
 ?
1.14.14.11 styrene + FADH2 + O2 StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity Rhodococcus opacus (S)-2-phenyloxirane + FAD + H2O
-
 ?
1.14.14.11 styrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (S)-2-phenyloxirane + FAD + H2O
-
 ?
1.14.14.11 styrene + FADH2 + O2 StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity Rhodococcus opacus 1CP (S)-2-phenyloxirane + FAD + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.11 dimer 2 * 44000, SDS-PAGE Rhodococcus opacus

Synonyms

EC Number Synonyms Comment Organism
1.14.14.11 StyA1
-
 Rhodococcus opacus
1.14.14.11 StyA1/StyA2B StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity Rhodococcus opacus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.11 FADH2 StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity Rhodococcus opacus