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Literature summary for 1.14.13.22 extracted from

  • Latham, J.A.; Branchaud, B.P.; Chen, Y.C.J.; Walsh, C.
    Allylic and propargylic phenyl selenide oxygenation by cyclohexanone oxygenase: [2,3]-sigmatropic rearrangement of the enzyme-generated selenoxide (1986), J. Chem. Soc. Chem. Commun., 1986, 528-530.
No PubMed abstract available
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0068
-
 trans-hex-2-enyl phenyl selenide
-
 Acinetobacter sp.
0.0096
-
 cis-hex-2-enyl phenyl selenide
-
 Acinetobacter sp.
0.128
-
 phenyl propargyl selenide
-
 Acinetobacter sp.

Organism

Organism UniProt Comment Textmining
Acinetobacter sp.
-
 NCIB 9871
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cis-hex-2-enyl phenyl selenide + NADPH + O2
-
 Acinetobacter sp. ?
-
 ?
additional information oxidation of propargylic and allylic selenides Acinetobacter sp. ?
-
 ?
phenyl propargyl selenide + NADPH + O2
-
 Acinetobacter sp. ?
-
 ?
trans-hex-2-enyl phenyl selenide + NADPH + O2
-
 Acinetobacter sp. ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.683
-
 cis-hex-2-enyl phenyl selenide
-
 Acinetobacter sp.
0.917
-
 trans-hex-2-enyl phenyl selenide
-
 Acinetobacter sp.
9.75
-
 phenyl propargyl selenide
-
 Acinetobacter sp.

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Acinetobacter sp.