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Literature summary for 1.14.13.16 extracted from

  • Trudgill, P.W.
    Cyclopentanone 1,2-monooxygenase from Pseudomonas N.C.I.B. 9872 (1990), Methods Enzymol., 188, 77-81.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
O2
-
Pseudomonas sp.
0.15
-
Cyclopentanone
-
Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
194000
-
ultracentrifugation Pseudomonas sp.
200000
-
-
Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclopentanone + NADPH + O2 Pseudomonas sp.
-
5-valerolactone + NADP+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
NCIB 9872
-

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
4.3 5
-
Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclopentanone + NADPH + O2
-
Pseudomonas sp. 5-valerolactone + NADP+ + H2O
-
?

Subunits

Subunits Comment Organism
trimer or tetramer 3 or 4 * 54000-58000, SDS-PAGE Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
FAD FAD : enzyme ratio is 2.2 to 3.5 Pseudomonas sp.