Biol. Chem. Hoppe-Seyler Vol. 374, pp. 1037-1046, November 1993 Microbial Metabolism of Quinoline and Related Compounds XX. Quinaldic Acid 4-Oxidoreductase from Pseudomonas sp. AK-2 Compared to other Procaryotic Molybdenum-Containing Hydroxylases Monika SAUTER, Barbara TSHISUAKA, Susanne FETZNER and Franz LINGENS Institut für Mikrobiologie der Universität Hohenheim (Received 27 July / 26 August 1993) Dedicated to Prof. Dr. H. Hellmann on the occasion of his 80th birthday Summary: Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 catalyses the hydroxylation of quinoline 2-carboxylic acid (quinaldic acid) to 4-hydroxyquinoline 2-carboxylic acid (kynurenic acid) with concomitant reduction of a suitable electron acceptor. An analogous hydroxylation in para-position relative to the N-heteroatom was only recently described for quinaldine 4-oxidoreductase (de Beyer & Lingens, 1993, Biol. Chem. Hoppe-Seyler 374, 101-110) and for quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1 (Fetzner & Lingens, 1993, Biol. Chem. Hoppe-Seyler 374, 363-376). Quinaldic acid 4-oxidoreductase from Pseudomonas putida AK-2 was purified 78-fold to electrophoretic homogeneity with a recovery of 22%. The native enzyme (300kDa) was composed of three subunits with molecular masses of 90, 34 and 20kDa, indicating an «2/8272 structure. Quinaldic acid 4-oxidoreductase contained FAD, molybdenum, iron and acid-labile sulfur in a ratio of 2:2:8:8. Molybdenum is probably associated
Biological Chemistry Hoppe-Seyler – de Gruyter
Published: Jan 1, 1993
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