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Literature summary for 1.13.12.2 extracted from

  • Nakazawa, T.
    Lysine oxygenase (Pseudomonas) (1971), Methods Enzymol., 17B, 154-157.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Pseudomonas fluorescens

Inhibitors

Inhibitors Comment Organism Structure
Hg2+
-
Pseudomonas fluorescens
Mersalyl
-
Pseudomonas fluorescens
o-Iodosobenzoate
-
Pseudomonas fluorescens
p-chloromercuribenzoate
-
Pseudomonas fluorescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Pseudomonas fluorescens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metals play no role in lysine monooxygenase Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
ATCC 11250
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas fluorescens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10.3
-
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 monooxygenase activity Pseudomonas fluorescens 5-aminopentanamide + CO2 + H2O
-
?
L-thialysine + O2 monooxygenase and oxidase activity Pseudomonas fluorescens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
34.7
-
L-lysine
-
Pseudomonas fluorescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
-
Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
FAD contains 2 mol of FAD per mol of enzyme Pseudomonas fluorescens