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Literature summary for 1.3.99.17 extracted from

  • Tshisuaka, B.; Kappl, R.; Huttermann, J.; Lingens, F.
    Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy (1993), Biochemistry, 32, 12928-12934.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mo clear correlation between the molybdenum cytosine dinucleotide molybdenum cofactor, the reduction of the enzyme by its substrate quinoline and the appearence of the Mo(V) rapid type Q EPR signal Pseudomonas putida
Mo the enzyme contains a molybdenum-molybdopterin cytosine dinucleotide cofactor Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
FAD contains FAD as cofactor Pseudomonas putida
molybdopterin molybdopterin cytosine dinucleotide is a part of the pterin molybdenum cofactor Pseudomonas putida