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Literature summary for 1.14.13.9 extracted from

  • Crozier, K.R.; Moran, G.R.
    Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400 (2007), Protein Expr. Purif., 51, 324-333.
    View publication on PubMed

Application

Application Comment Organism
medicine the enzyme is an attractive target for the treatment of ischemic stroke Pseudomonas fluorescens

Cloned(Commentary)

Cloned (Comment) Organism
functional expression in Escherichia coli strain BL21 (DE3) Pseudomonas fluorescens

General Stability

General Stability Organism
disulfide reductants like dithiothreitol or 2-mercaptoethanol stabilize the enzyme Pseudomonas fluorescens

Inhibitors

Inhibitors Comment Organism Structure
3-nitrobenzoylalanine
-
Pseudomonas fluorescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics and ligand perturbation of flavin fluorescence, overview Pseudomonas fluorescens
0.0085
-
NADPH recombinant enzyme, pH 7.5, 5°C Pseudomonas fluorescens
0.012
-
kynurenine recombinant enzyme, pH 7.5, 5°C Pseudomonas fluorescens
0.034
-
O2 recombinant enzyme, pH 7.5, 5°C Pseudomonas fluorescens
0.053
-
kynurenine recombinant enzyme, pH 7.5, 25°C Pseudomonas fluorescens
0.071
-
O2 recombinant enzyme, pH 7.5, 25°C Pseudomonas fluorescens
0.091
-
NADPH recombinant enzyme, pH 7.5, 25°C Pseudomonas fluorescens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
x * 50000, recombinant enzyme, SDS-PAGE Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
kynurenine + NADPH + O2 Pseudomonas fluorescens the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate 3-hydroxy-kynurenine + NADP+ + H2O the product acts as apoptotic signal ir
kynurenine + NADPH + O2 Pseudomonas fluorescens 17400 the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate 3-hydroxy-kynurenine + NADP+ + H2O the product acts as apoptotic signal ir

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-
Pseudomonas fluorescens 17400
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme 8.8fold from Escherichia coli strain by ammonium sulfate fractionation and ion exchange chromatography to homogeneity Pseudomonas fluorescens

Source Tissue

Source Tissue Comment Organism Textmining
microglia
-
Pseudomonas fluorescens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.15
-
purified recombinant enzyme Pseudomonas fluorescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
kynurenine + NADPH + O2 the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate Pseudomonas fluorescens 3-hydroxy-kynurenine + NADP+ + H2O the product acts as apoptotic signal ir
kynurenine + NADPH + O2 enzyme activity depends on the reduction state of the enzyme Pseudomonas fluorescens 3-hydroxy-kynurenine + NADP+ + H2O
-
ir
kynurenine + NADPH + O2 the reaction is central to the tryptophan degradative pathway, overview, and takes place within microglial cells defining cellular concentrations of the N-methyl-D-aspatate receptor agonist quinolinate and antagonist kynurenate Pseudomonas fluorescens 17400 3-hydroxy-kynurenine + NADP+ + H2O the product acts as apoptotic signal ir
kynurenine + NADPH + O2 enzyme activity depends on the reduction state of the enzyme Pseudomonas fluorescens 17400 3-hydroxy-kynurenine + NADP+ + H2O
-
ir

Subunits

Subunits Comment Organism
? x * 50000, recombinant enzyme, SDS-PAGE Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
KMO
-
Pseudomonas fluorescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas fluorescens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3
-
kynurenine recombinant enzyme, pH 7.5, 5°C Pseudomonas fluorescens
4.9
-
kynurenine recombinant enzyme, pH 7.5, 25°C Pseudomonas fluorescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Pseudomonas fluorescens

pH Range

pH Minimum pH Maximum Comment Organism
7.2 9.7
-
Pseudomonas fluorescens

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 7 purified recombinant enzyme, 4°C, stable Pseudomonas fluorescens
8
-
purified recombinant enzyme, 4°C, 10 h, loss of 21% of activity Pseudomonas fluorescens
9
-
purified recombinant enzyme, 4°C, 10 h, loss of 32% of activity Pseudomonas fluorescens
10
-
purified recombinant enzyme, 4°C, 3 h, complete inactivation Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Pseudomonas fluorescens
NADPH dependent on Pseudomonas fluorescens