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Literature summary for 1.14.14.11 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
Search for more literature for 1.14.14.11

Cloned(Commentary)

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus C7ACG0 StyA1
-
Rhodococcus opacus 1CP C7ACG0 StyA1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rhodococcus opacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
-
 ?
2-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O
-
 ?
3-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
-
 ?
3-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O
-
 ?
4-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
-
 ?
4-chlorostyrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O
-
 ?
4-methylstyrene + FADH2 + O2
-
 Rhodococcus opacus ? + FAD + H2O
-
 ?
styrene + FADH2 + O2
-
 Rhodococcus opacus (S)-2-phenyloxirane + FAD + H2O
-
 ?
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
-
 ?
styrene + FADH2 + O2
-
 Rhodococcus opacus 1CP (S)-2-phenyloxirane + FAD + H2O
-
 ?
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

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

Synonyms

Synonyms Comment Organism
StyA1
-
 Rhodococcus opacus
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

Cofactor Comment Organism Structure
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