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- W2322851930 abstract "The quinoline oxidoreductase from Pseudomonas putida was purified 50-fold to homogeneity with 21% recovery, using ammonium sulfate precipitation, hydrophobic interaction-, anion exchange-, and gel chromatography. The Mr of the native enzyme was calculated to be 300,000 by gel filtration. SDS-polyacrylamide gel electrophoresis of the enzyme revealed three protein bands corresponding to Mr 85,000, 30,000 and 20,000. The enzyme contained 8 atoms of iron, 8 atoms of acid-labile sulfide, 2 molecules of FAD, and the molybdenum cofactor, molybdopterin. Besides quinoline, the quinoline oxidoreductase also catalysed the conversion of 5-, 6-, 7- and 8-hydroxyquinoline and 8-chloroquinoline to the corresponding 2-oxo compounds. The incorporated oxygen atom was derived from water. Cyanide and methanol were effective inhibitors." @default.
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- W2322851930 date "1990-01-01" @default.
- W2322851930 modified "2023-10-11" @default.
- W2322851930 title "Microbial Metabolism of Quinoline and Related Compounds. VII. Quinoline Oxidoreductase from<i>Pseudomonas putida</i>: a Molybdenum-Containing Enzyme" @default.
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- W2322851930 doi "https://doi.org/10.1515/bchm3.1990.371.2.1137" @default.
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