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- W2015084067 abstract "The quinoline-4-carboxylic acid oxidoreductase from Agrobacterium spec.1B was purified 84-fold to apparent homogeneity with 15% recovery, using ammonium sulphate precipitation, heat precipitation, hydrophobic interaction, anion exchange- and gel chromatography. The molecular mass of the native enzyme was estimated to be 320 kDa by gel filtration. SDS-polyacrylamide gel electrophoresis of the enzyme revealed three protein bands corresponding to 85, 35 and 21 kDa. Per molecule the enzyme contains 8 atoms of iron, 8 atoms of acid-labile sulphur, 2 atoms of molybdenum, 2 molecules of FAD and as molybdenum cofactor, molybdopterin cytosine dinucleotide. Besides quinoline-4-carboxylic acid the enzyme also catalysed the conversion of quinoline, 4-chloroquinoline and 4-methylquinoline to the corresponding 2-oxo-1,2-dihydroderivatives. Cyanide, methanol, 4-chloromercuribenzoate and acriflavin were effective inhibitors." @default.
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- W2015084067 date "1992-01-01" @default.
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- W2015084067 title "Microbial Metabolism of Quinoline and Related Compounds. XV. Quinoline-4-carboxylic acid Oxidoreductase from<i>Agrobacterium spec.1B:</i>A Molybdenum-Containing Enzyme" @default.
- W2015084067 doi "https://doi.org/10.1515/bchm3.1992.373.2.699" @default.
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