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Literature summary for 1.14.14.11 extracted from

  • Ukaegbu, U.E.; Kantz, A.; Beaton, M.; Gassner, G.T.; Rosenzweig, A.C.
    Structure and ligand binding properties of the epoxidase component of styrene monooxygenase (2010), Biochemistry, 49, 1678-1688.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.14.11

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
styrene + FADH2 + O2 Pseudomonas putida
-
 (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 Pseudomonas putida S12
-
 (S)-2-phenyloxirane + FAD + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida O33471
-
-
Pseudomonas putida S12 O33471
-
-

Purification (Commentary)

Purification (Comment) Organism
N-terminally histidine-tagged styrene monooxygenase Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
styrene + FADH2 + O2
-
 Pseudomonas putida (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene Pseudomonas putida (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2
-
 Pseudomonas putida S12 (S)-2-phenyloxirane + FAD + H2O
-
 ?
styrene + FADH2 + O2 preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene Pseudomonas putida S12 (S)-2-phenyloxirane + FAD + H2O
-
 ?

Subunits

Subunits Comment Organism
homodimer each monomer forms two distinct domains Pseudomonas putida

Synonyms

Synonyms Comment Organism
NSMOA
-
 Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FADH2 flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA about 8000times more tightly than the oxidized coenzyme Pseudomonas putida