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Literature summary 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

EC Number Metals/Ions Comment Organism Structure
1.3.99.17 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
1.3.99.17 Mo the enzyme contains a molybdenum-molybdopterin cytosine dinucleotide cofactor Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.3.99.17 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.99.17
-
Pseudomonas putida

Cofactor

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