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Literature summary for 1.14.12.16 extracted from

  • Schach, S.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
    Quinoline 2-oxidoreductase and 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase from Comamonas testosteroni 63. The first two enzymes in quinoline and 3-methylquinoline degradation (1995), Eur. J. Biochem., 232, 536-544.
    View publication on PubMed
Search for more literature for 1.14.12.16

General Stability

General Stability Organism
dithioerythritol, dithiothreitol and 2-oxo-1,2-dihydroquinoline stabilize Comamonas testosteroni

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 0.5 mM, 82% loss of activity Comamonas testosteroni
4-hydroxymercuribenzoate 0.1 mM, complete loss of activity Comamonas testosteroni
Acriflavin 0.5 mM, 69% loss of activity Comamonas testosteroni
Cu2+
-
 Comamonas testosteroni
diethyldithiocarbaminate inhibits after a prolonged incubation time Comamonas testosteroni
EDTA inhibits after a prolonged incubation time Comamonas testosteroni
iodoacetate 2 mM, complete loss of activity Comamonas testosteroni
NaCl 0.2 M, 50% loss of activity Comamonas testosteroni
Quinacrine 0.5 mM, 15% loss of activity Comamonas testosteroni

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enhances activity 1.5fold Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Comamonas testosteroni second enzyme in the pathway of quinoline and 3-methylquinoline degradation ?
-
 ?
additional information Comamonas testosteroni 63 second enzyme in the pathway of quinoline and 3-methylquinoline degradation ?
-
 ?

Organic Solvent Stability

Organic Solvent Comment Organism
Ethanol 5%, decreases enzyme activity to 44% Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
-
-
Comamonas testosteroni 63
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Comamonas testosteroni

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.125
-
-
 Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
 Comamonas testosteroni ?
-
 ?
2-Oxo-1,2-dihydroquinoline + NADH + O2
-
 Comamonas testosteroni 63 ?
-
 ?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2 NADH cannot be replaced by NADPH Comamonas testosteroni 5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
 ?
3-Methyl-2-oxo-1,2-dihydroquinoline + NADH + O2 NADH cannot be replaced by NADPH Comamonas testosteroni 63 5,6-Dihydro-5,6-dihydroxy-(3-methyl-)2-oxo-1,2-dihydroquinoline + NAD+
-
 ?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
 Comamonas testosteroni ?
-
 ?
6-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
 Comamonas testosteroni 63 ?
-
 ?
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NADH + O2
-
 Comamonas testosteroni ?
-
 ?
8-Hydroxyquinoline + NADH + O2
-
 Comamonas testosteroni ?
-
 ?
8-Hydroxyquinoline + NADH + O2
-
 Comamonas testosteroni 63 ?
-
 ?
additional information second enzyme in the pathway of quinoline and 3-methylquinoline degradation Comamonas testosteroni ?
-
 ?
additional information second enzyme in the pathway of quinoline and 3-methylquinoline degradation Comamonas testosteroni 63 ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 5 min, 30% loss of activity Comamonas testosteroni
65
-
 5 min, complete loss of activity Comamonas testosteroni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Comamonas testosteroni

Cofactor

Cofactor Comment Organism Structure
NADH required, cannot be replaced by NADPH Comamonas testosteroni